|
|
| Line 7: |
Line 7: |
| | Prostate cancer | | Prostate cancer |
| | Activity Androgen | | Activity Androgen |
| - | MMDB ID: 13575 | + | {| border="1;width:100%; height:200px;style=text-align:center" |
| - | PDB ID: 1D2S | + | |+'''Table I:''' |
| - | Reference: Grishkovskaya I, Avvakumov GV, Sklenar G, Dales D, Hammond GL, Muller YACrystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domainEMBO J. v19, p.504-512
| + | |- |
| - | Human sex hormone-binding globulin (SHBG) transports sex steroids in blood and regulates their access to target tissues. In biological fluids, SHBG exists as a homodimer and each monomer comprises two laminin G-like domains (G domains). The crystal structure of the N-terminal G domain of SHBG in complex with 5alpha-dihydrotestosterone at 1.55 A resolution reveals both the architecture of the steroid-binding site and the quaternary structure of the dimer....
| + | ! style="background:brown; color:white" |MMDB ID |
| - | | + | ! style="background:brown; color:white" |PDB ID |
| - | MMDB ID: 13985
| + | ! style="background:brown; color:white" |Reference |
| - | PDB ID: 1F5F
| + | |- |
| - | Reference: Avvakumov GV, Muller YA, Hammond GLSteroid-binding specificity of human sex hormone-binding globulin is influenced by occupancy of a zinc-binding siteJ. Biol. Chem. v275, p.25920-25925
| + | |13575 |
| - | One calcium-binding site (site I) and a second poorly defined metal-binding site (site II) have been observed previously within the amino-terminal laminin G-like domain (G domain) of human sex hormone-binding globulin (SHBG). By soaking crystals of this structure in 2.5 mm ZnCl(2), site II and a new metal-binding site (site III) were found to bind Zn(2+)....
| + | |1D2S |
| - | | + | |Grishkovskaya I, Avvakumov GV, Sklenar G, Dales D, Hammond GL, Muller YACrystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domainEMBO J. v19, p.504-512 |
| - | MMDB ID: 19532
| + | |- |
| - | PDB ID: 1KDK
| + | |13985 |
| - | Reference: Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YAResolution of a disordered region at the entrance of the human sex hormone-binding globulin steroid-binding siteJ. Mol. Biol. v318, p.621-626
| + | |1F5F |
| - | The crystal structure of human sex hormone-binding globulin (SHBG) has revealed how 5alpha-dihydrotestosterone intercalates between the two seven-stranded beta-sheets of its amino-terminal laminin G-like domain. However, a region of disorder (residues 130 to 135 of SHBG) was identified together with a zinc-binding site in immediate proximity to the steroid....
| + | |Avvakumov GV, Muller YA, Hammond GLSteroid-binding specificity of human sex hormone-binding globulin is influenced by occupancy of a zinc-binding siteJ. Biol. Chem. v275, p.25920-25925 |
| - | | + | |- |
| - | MMDB ID: 19533
| + | |19532 |
| - | PDB ID: 1KDM
| + | |1KDK |
| - | Reference: Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YAResolution of a disordered region at the entrance of the human sex hormone-binding globulin steroid-binding siteJ. Mol. Biol. v318, p.621-626
| + | |Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YAResolution of a disordered region at the entrance of the human sex hormone-binding globulin steroid-binding siteJ. Mol. Biol. v318, p.621-626 |
| - | The crystal structure of human sex hormone-binding globulin (SHBG) has revealed how 5alpha-dihydrotestosterone intercalates between the two seven-stranded beta-sheets of its amino-terminal laminin G-like domain. However, a region of disorder (residues 130 to 135 of SHBG) was identified together with a zinc-binding site in immediate proximity to the steroid....
| + | |- |
| - | | + | |19533 |
| - | MMDB ID: 29012
| + | |1KDM |
| - | PDB ID: 1T73
| + | |Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YAResolution of a disordered region at the entrance of the human sex |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |29012 |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |- |
| - | | + | |1T73 |
| - | MMDB ID: 29013
| + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | PDB ID: 1T74
| + | |- |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |29013 |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |1T74 |
| - | | + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor |
| - | MMDB ID: 29014
| + | |- |
| - | PDB ID: 1T76
| + | |29014 |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |1T76 |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | | + | |- |
| - | MMDB ID: 29015
| + | |29015 |
| - | PDB ID: 1T79
| + | |1T79 |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |- |
| - | | + | |29016 |
| - | MMDB ID: 29016
| + | |1T7F |
| - | PDB ID: 1T7F
| + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |- |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |29017 |
| - | | + | |1T7M |
| - | MMDB ID: 29017
| + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | PDB ID: 1T7M
| + | |- |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |29018 |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |1T7R |
| - | | + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | MMDB ID: 29018
| + | |- |
| - | PDB ID: 1T7R
| + | |29019 |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |1T7T |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274 |
| - | | + | |- |
| - | MMDB ID: 29019
| + | |31245 |
| - | PDB ID: 1T7T
| + | |1T5Z |
| - | Reference: Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
| + | |Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068 |
| - | Prostate cancer is a leading killer of men in the industrialized world. Underlying this disease is the aberrant action of the androgen receptor (AR). AR is distinguished from other nuclear receptors in that after hormone binding, it preferentially responds to a specialized set of coactivators bearing aromatic-rich motifs, while responding poorly to coactivators bearing the leucine-rich "NR box" motifs favored by other nuclear receptors....
| + | |- |
| - | | + | |31246 |
| - | MMDB ID: 31245
| + | |1T63 |
| - | PDB ID: 1T5Z
| + | |Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068 |
| - | Reference: Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
| + | |- |
| - | Androgens drive sex differentiation, bone and muscle development, and promote growth of hormone-dependent cancers by binding the nuclear androgen receptor (AR), which recruits coactivators to responsive genes. Most nuclear receptors recruit steroid receptor coactivators (SRCs) to their ligand binding domain (LBD) using a leucine-rich motif (LXXLL)....
| + | |31247 |
| - | | + | |1T65 |
| - | MMDB ID: 31246
| + | |Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068 |
| - | PDB ID: 1T63
| + | |- |
| - | Reference: Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
| + | |31438 |
| - | Androgens drive sex differentiation, bone and muscle development, and promote growth of hormone-dependent cancers by binding the nuclear androgen receptor (AR), which recruits coactivators to responsive genes. Most nuclear receptors recruit steroid receptor coactivators (SRCs) to their ligand binding domain (LBD) using a leucine-rich motif (LXXLL)....
| + | |1XJ7 |
| - | | + | |Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068 |
| - | MMDB ID: 31247
| + | |- |
| - | PDB ID: 1T65
| + | |39038 |
| - | Reference: Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
| + | |2AMA |
| - | Androgens drive sex differentiation, bone and muscle development, and promote growth of hormone-dependent cancers by binding the nuclear androgen receptor (AR), which recruits coactivators to responsive genes. Most nuclear receptors recruit steroid receptor coactivators (SRCs) to their ligand binding domain (LBD) using a leucine-rich motif (LXXLL)....
| + | |Pereira de Je, Cote PL, Cantin L, Blanchet J, Labrie F, Breton RComparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinityProtein Sci. v15, p.987-999 |
| - | | + | |- |
| - | MMDB ID: 31438
| + | |59291 |
| - | PDB ID: 1XJ7
| + | |2PIO |
| - | Reference: Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | Androgens drive sex differentiation, bone and muscle development, and promote growth of hormone-dependent cancers by binding the nuclear androgen receptor (AR), which recruits coactivators to responsive genes. Most nuclear receptors recruit steroid receptor coactivators (SRCs) to their ligand binding domain (LBD) using a leucine-rich motif (LXXLL)....
| + | |- |
| - | | + | |59292 |
| - | MMDB ID: 39038
| + | |2PIP |
| - | PDB ID: 2AMA
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | Reference: Pereira de Je, Cote PL, Cantin L, Blanchet J, Labrie F, Breton RComparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinityProtein Sci. v15, p.987-999
| + | |- |
| - | Androgens exert their effects by binding to the highly specific androgen receptor (AR). In addition to natural potent androgens, AR binds a variety of synthetic agonist or antagonist molecules with different affinities. To identify molecular determinants responsible for this selectivity, we have determined the crystal structure of the human androgen receptor ligand-binding domain (hARLBD) in complex with two natural androgens, testosterone (Testo) and dihydrotestosterone (DHT), and with an androgenic steroid used in sport doping, tetrahydrogestrinone (THG), at 1.64, 1.90, and 1.75 A resolution,
| + | |59293 |
| - | | + | |2PIQ |
| - | MMDB ID: 59291
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | PDB ID: 2PIO
| + | |- |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |59294 |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |2PIR |
| - | | + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | MMDB ID: 59292
| + | |- |
| - | PDB ID: 2PIP
| + | |59295 |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |2PIT |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | | + | |- |
| - | MMDB ID: 59293
| + | |59296 |
| - | PDB ID: 2PIQ
| + | |2PIU |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |- |
| - | | + | |59297 |
| - | MMDB ID: 59294
| + | |2PIV |
| - | PDB ID: 2PIR
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |- |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |59298 |
| - | | + | |2PIW |
| - | MMDB ID: 59295
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | PDB ID: 2PIT
| + | |- |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |59299 |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |2PIX |
| - | | + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | MMDB ID: 59296
| + | |- |
| - | PDB ID: 2PIU
| + | |59302 |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |2PKL |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | | + | |- |
| - | MMDB ID: 59297
| + | |59526 |
| - | PDB ID: 2PIV
| + | |2QPY |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079 |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |- |
| - | | + | |61083 |
| - | MMDB ID: 59298
| + | |2Z4J |
| - | PDB ID: 2PIW
| + | |Jouravel N, Sablin E, Arnold LA, Guy RK, Fletterick RJInteraction between the androgen receptor and a segment of its corepressor SHPActa Crystallogr. D Biol. Crystallogr. v63, p.1198-1200 |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |- |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |} |
| - | | + | |
| - | MMDB ID: 59299
| + | |
| - | PDB ID: 2PIX
| + | |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |
| - | | + | |
| - | MMDB ID: 59302
| + | |
| - | PDB ID: 2PKL
| + | |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |
| - | | + | |
| - | MMDB ID: 59526
| + | |
| - | PDB ID: 2QPY
| + | |
| - | Reference: Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
| + | |
| - | Current approaches to inhibit nuclear receptor (NR) activity target the hormone binding pocket but face limitations. We have proposed that inhibitors, which bind to nuclear receptor surfaces that mediate assembly of the receptor"s binding partners, might overcome some of these limitations. The androgen receptor (AR) plays a central role in prostate cancer, but conventional inhibitors lose effectiveness as cancer treatments because anti-androgen resistance usually develops....
| + | |
| - | | + | |
| - | MMDB ID: 61083
| + | |
| - | PDB ID: 2Z4J
| + | |
| - | Reference: Jouravel N, Sablin E, Arnold LA, Guy RK, Fletterick RJInteraction between the androgen receptor and a segment of its corepressor SHPActa Crystallogr. D Biol. Crystallogr. v63, p.1198-1200
| + | |
| - | The mechanisms of functional repression of the androgen receptor (AR) are crucial for the regulation of genes involved in physiological development as well as for the progression of prostate cancer. To date, only two in vivo inhibitors of AR-mediated transcription have been identified: DAX-1 and SHP (small heterodimer partner)....
| + | |
| | | | |
| | Physical Property Value Units Temp (deg C) Source | | Physical Property Value Units Temp (deg C) Source |
Androstanolone(DHT)
Pubchem(10635)
A potent androgenic metabolite of TESTOSTERONE. Dihydrotestosterone (DHT) is generated by a 5-alpha reduction of testosterone. Unlike testosterone, DHT cannot be aromatized to ESTRADIOL therefore DHT is considered a pure androgenic steroid.
KEGG Pathway(C03917,
Pathway
Androgen and estrogen metabolism
Prostate cancer
Activity Androgen
Table I:
| MMDB ID
| PDB ID
| Reference
|
| 13575
| 1D2S
| Grishkovskaya I, Avvakumov GV, Sklenar G, Dales D, Hammond GL, Muller YACrystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domainEMBO J. v19, p.504-512
|
| 13985
| 1F5F
| Avvakumov GV, Muller YA, Hammond GLSteroid-binding specificity of human sex hormone-binding globulin is influenced by occupancy of a zinc-binding siteJ. Biol. Chem. v275, p.25920-25925
|
| 19532
| 1KDK
| Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YAResolution of a disordered region at the entrance of the human sex hormone-binding globulin steroid-binding siteJ. Mol. Biol. v318, p.621-626
|
| 19533
| 1KDM
| Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YAResolution of a disordered region at the entrance of the human sex
| 29012
|
| 1T73
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 29013
| 1T74
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor
|
| 29014
| 1T76
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 29015
| 1T79
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 29016
| 1T7F
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 29017
| 1T7M
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 29018
| 1T7R
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 29019
| 1T7T
| Hur E, Pfaff SJ, Payne ES, Gron H, Buehrer BM, Fletterick RJRecognition and accommodation at the androgen receptor coactivator binding interfacePLoS Biol. v2, p.E274
|
| 31245
| 1T5Z
| Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
|
| 31246
| 1T63
| Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
|
| 31247
| 1T65
| Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
|
| 31438
| 1XJ7
| Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RKThe molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptorJ. Biol. Chem. v280, p.8060-8068
|
| 39038
| 2AMA
| Pereira de Je, Cote PL, Cantin L, Blanchet J, Labrie F, Breton RComparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinityProtein Sci. v15, p.987-999
|
| 59291
| 2PIO
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59292
| 2PIP
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59293
| 2PIQ
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59294
| 2PIR
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59295
| 2PIT
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59296
| 2PIU
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59297
| 2PIV
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59298
| 2PIW
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59299
| 2PIX
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59302
| 2PKL
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 59526
| 2QPY
| Estebanez-Perpina E, Arnold LA, Nguyen P, Rodrigues ED, Mar E, Bateman R, Pallai P, Shokat KM, Baxter JD, Guy RK, Webb P, Fletterick RJA surface on the androgen receptor that allosterically regulates coactivator bindingProc. Natl. Acad. Sci. U. S. A. v104, p.16074-16079
|
| 61083
| 2Z4J
| Jouravel N, Sablin E, Arnold LA, Guy RK, Fletterick RJInteraction between the androgen receptor and a segment of its corepressor SHPActa Crystallogr. D Biol. Crystallogr. v63, p.1198-1200
|
Physical Property Value Units Temp (deg C) Source
Melting Point 181 deg C EXP
log P (octanol-water) 3.55 (none) EXP
Water Solubility 5.25E+05 mg/L 25 EXP
Vapor Pressure 2.79E-08 mm Hg 25 EST
Henry's Law Constant 6.37E-09 atm-m3/mole 25 EST
Atmospheric OH Rate Constant 4.17E-11 cm3/molecule-sec 25 EST
