Testosterone

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	KEGG Pathway(C00535,D00075)		KEGG Pathway(C00535,D00075)
-	Androgen and estrogen metabolism	+	*Androgen and estrogen metabolism
-	Prostate cancer	+	*Prostate cancer
		+
	Activity Androgen		Activity Androgen
		+	{| border="1;width:100%; height:200px;style=text-align:center"
		+	|+'''List of PDB files having estradiol as a Ligand:'''
		+	|-
		+	! style="background:brown; color:white" |MMDB ID
		+	! style="background:brown; color:white" |PDB ID
		+	! style="background:brown; color:white" |Reference
		+	|-
	|15896		|15896
	|1I37		|1I37

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Revision as of 05:47, 30 October 2008

Testosterone Pubchem(6013) A potent androgenic steroid and major product secreted by the LEYDIG CELLS of the TESTIS. Its production is stimulated by LUTEINIZING HORMONE from the PITUITARY GLAND. In turn, testosterone exerts feedback control of the pituitary LH and FSH secretion. Depending on the tissues, testosterone can be further converted to DIHYDROTESTOSTERONE or ESTRADIOL.

KEGG Pathway(C00535,D00075)

• Androgen and estrogen metabolism
• Prostate cancer

Activity Androgen

Physical Property Value Units Temp (deg C) Source Melting Point 155 deg C EXP log P (octanol-water) 3.32 (none) EXP Water Solubility 23.4 mg/L 25 EXP Vapor Pressure 2.23E-08 mm Hg 25 EST Henry's Law Constant 3.53E-09 atm-m3/mole 25 EST Atmospheric OH Rate Constant 1.07E-10 cm3/molecule-sec 25 EST Organism Test Type Route Reported Dose (Normalized Dose) Effect Source mammal (species unspecified) LD50 oral > 5gm/kg (5000mg/kg) Toksikologicheskii Vestnik. Vol. (2), Pg. 6, 1996. rat LDLo intraperitoneal 326mg/kg (326mg/kg) LUNGS, THORAX, OR RESPIRATION: OTHER CHANGES Proceedings of the Society for Experimental Biology and Medicine. Vol. 46, Pg. 116, 1941.

List of PDB files having estradiol as a Ligand:

MMDB ID	PDB ID	Reference
15896	1I37	Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909
15897	1I38	Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HMCrystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosteroneProc. Natl. Acad. Sci. U. S. A. v98, p.4904-4909
18740	1I9J	Valjakka J, Takkinenz K, Teerinen T, Soderlund H, Rouvinen JStructural insights into steroid hormone binding: the crystal structure of a recombinant anti-testosterone Fab fragment in free and testosterone-bound formsJ. Biol. Chem. v277, p.4183-4190
19484	1J96	Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SXStructure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolutionJ. Biol. Chem. v276, p.42091-42098
30244	1Q13	Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton RLoop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamilyJ. Mol. Biol. v339, p.89-102
30428	1VPO	Valjakka J, Hemminki A, Niemi S, Soderlund H, Takkinen K, Rouvinen JCrystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domainsJ. Biol. Chem. v277, p.44021-44027
54139	2Q7I	Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
54140	2Q7J	Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
54141	2Q7K	Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
54142	2Q7L	Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EMModulation of androgen receptor activation function 2 by testosterone and dihydrotestosteroneJ. Biol. Chem. v282, p.25801-25816
6729	1AFS	Bennett MJ, Albert RH, Jez JM, Ma H, Penning TM, Lewis MSteroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenaseStructure v5, p.799-812