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PDBsum entry 3g0w

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protein ligands links
Hormone PDB id
3g0w
Jmol
Contents
Protein chain
249 a.a. *
Ligands
LGB
Waters ×171
* Residue conservation analysis
PDB id:
3g0w
Name: Hormone
Title: Crystal structure of the rat androgen receptor ligand binding domain complex with an n-aryl-oxazolidin 2-imine inhibitor
Structure: Androgen receptor. Chain: a. Fragment: ligand-binding domain. Synonym: dihydrotestosterone receptor, nuclear receptor subfamily 3 group c member 4. Engineered: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: ar, nr3c4. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.95Å     R-factor:   0.201     R-free:   0.238
Authors: J.S.Sack
Key ref: A.A.Nirschl et al. (2009). N-aryl-oxazolidin-2-imine muscle selective androgen receptor modulators enhance potency through pharmacophore reorientation. J Med Chem, 52, 2794-2798. PubMed id: 19351168 DOI: 10.1021/jm801583j
Date:
29-Jan-09     Release date:   28-Apr-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P15207  (ANDR_RAT) -  Androgen receptor
Seq:
Struc:
 
Seq:
Struc:
902 a.a.
249 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     steroid hormone mediated signaling pathway   2 terms 
  Biochemical function     DNA binding     3 terms  

 

 
DOI no: 10.1021/jm801583j J Med Chem 52:2794-2798 (2009)
PubMed id: 19351168  
 
 
N-aryl-oxazolidin-2-imine muscle selective androgen receptor modulators enhance potency through pharmacophore reorientation.
A.A.Nirschl, Y.Zou, S.R.Krystek, J.C.Sutton, L.M.Simpkins, J.A.Lupisella, J.E.Kuhns, R.Seethala, R.Golla, P.G.Sleph, B.C.Beehler, G.J.Grover, D.Egan, A.Fura, V.P.Vyas, Y.X.Li, J.S.Sack, K.F.Kish, Y.An, J.A.Bryson, J.Z.Gougoutas, J.DiMarco, R.Zahler, J.Ostrowski, L.G.Hamann.
 
  ABSTRACT  
 
A novel selective androgen receptor modulator (SARM) scaffold was discovered as a byproduct obtained during synthesis of our earlier series of imidazolidin-2-ones. The resulting oxazolidin-2-imines are among the most potent SARMs known, with many analogues exhibiting sub-nM in vitro potency in binding and functional assays. Despite the potential for hydrolytic instability at gut pH, compounds of the present class showed good oral bioavailability and were highly active in a standard rodent pharmacological model.