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2nw4

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[[Image:2nw4.gif|left|200px]]<br /><applet load="2nw4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2nw4.gif|left|200px]]
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caption="2nw4, resolution 3.00&Aring;" />
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'''Crystal Structure of the Rat Androgen Receptor Ligand Binding Domain Complex with BMS-564929'''<br />
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{{Structure
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|PDB= 2nw4 |SIZE=350|CAPTION= <scene name='initialview01'>2nw4</scene>, resolution 3.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=8NH:2-CHLORO-4-[(7R,7AS)-7-HYDROXY-1,3-DIOXOTETRAHYDRO-1H-PYRROLO[1,2-C]IMIDAZOL-2(3H)-YL]-3-METHYLBENZONITRILE'>8NH</scene>
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|ACTIVITY=
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|GENE= Ar, Nr3c4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''Crystal Structure of the Rat Androgen Receptor Ligand Binding Domain Complex with BMS-564929'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2NW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=8NH:'>8NH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NW4 OCA].
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2NW4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NW4 OCA].
==Reference==
==Reference==
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Pharmacological and x-ray structural characterization of a novel selective androgen receptor modulator: potent hyperanabolic stimulation of skeletal muscle with hypostimulation of prostate in rats., Ostrowski J, Kuhns JE, Lupisella JA, Manfredi MC, Beehler BC, Krystek SR Jr, Bi Y, Sun C, Seethala R, Golla R, Sleph PG, Fura A, An Y, Kish KF, Sack JS, Mookhtiar KA, Grover GJ, Hamann LG, Endocrinology. 2007 Jan;148(1):4-12. Epub 2006 Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17008401 17008401]
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Pharmacological and x-ray structural characterization of a novel selective androgen receptor modulator: potent hyperanabolic stimulation of skeletal muscle with hypostimulation of prostate in rats., Ostrowski J, Kuhns JE, Lupisella JA, Manfredi MC, Beehler BC, Krystek SR Jr, Bi Y, Sun C, Seethala R, Golla R, Sleph PG, Fura A, An Y, Kish KF, Sack JS, Mookhtiar KA, Grover GJ, Hamann LG, Endocrinology. 2007 Jan;148(1):4-12. Epub 2006 Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17008401 17008401]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:51:52 2008''

Revision as of 15:51, 20 March 2008


PDB ID 2nw4

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands:
Gene: Ar, Nr3c4 (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Rat Androgen Receptor Ligand Binding Domain Complex with BMS-564929


Overview

A novel, highly potent, orally active, nonsteroidal tissue selective androgen receptor (AR) modulator (BMS-564929) has been identified, and this compound has been advanced to clinical trials for the treatment of age-related functional decline. BMS-564929 is a subnanomolar AR agonist in vitro, is highly selective for the AR vs. other steroid hormone receptors, and exhibits no significant interactions with SHBG or aromatase. Dose response studies in castrated male rats show that BMS-564929 is substantially more potent than testosterone (T) in stimulating the growth of the levator ani muscle, and unlike T, highly selective for muscle vs. prostate. Key differences in the binding interactions of BMS-564929 with the AR relative to the native hormones were revealed through x-ray crystallography, including several unique contacts located in specific helices of the ligand binding domain important for coregulatory protein recruitment. Results from additional pharmacological studies effectively exclude alternative mechanistic contributions to the observed tissue selectivity of this unique, orally active androgen. Because concerns regarding the potential hyperstimulatory effects on prostate and an inconvenient route of administration are major drawbacks that limit the clinical use of T, the potent oral activity and tissue selectivity exhibited by BMS-564929 are expected to yield a clinical profile that provides the demonstrated beneficial effects of T in muscle and other tissues with a more favorable safety window.

About this Structure

2NW4 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Pharmacological and x-ray structural characterization of a novel selective androgen receptor modulator: potent hyperanabolic stimulation of skeletal muscle with hypostimulation of prostate in rats., Ostrowski J, Kuhns JE, Lupisella JA, Manfredi MC, Beehler BC, Krystek SR Jr, Bi Y, Sun C, Seethala R, Golla R, Sleph PG, Fura A, An Y, Kish KF, Sack JS, Mookhtiar KA, Grover GJ, Hamann LG, Endocrinology. 2007 Jan;148(1):4-12. Epub 2006 Sep 28. PMID:17008401

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