1i37
From Proteopedia
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CRYSTAL STRUCTURE OF THE RAT ANDROGEN RECEPTOR LIGAND BINDING DOMAIN COMPLEX WITH DIHYDROTESTOSTERONE
Overview
The structures of the ligand-binding domains (LBD) of the wild-type, androgen receptor (AR) and the T877A mutant corresponding to that in LNCaP, cells, both bound to dihydrotestosterone, have been refined at 2.0 A, resolution. In contrast to the homodimer seen in the retinoid-X receptor, and estrogen receptor LBD structures, the AR LBD is monomeric, possibly, because of the extended C terminus of AR, which lies in a groove at the, dimerization interface. Binding of the natural ligand dihydrotestosterone, by the mutant LBD involves interactions with the same residues as in the, wild-type receptor, with the exception of the side chain of threonine 877, which is an alanine residue in the mutant. This structural difference in, the binding pocket can explain the ability of the mutant AR found in LNCaP, cells (T877A) to accommodate progesterone and other ligands that the, wild-type receptor cannot.
About this Structure
1I37 is a Single protein structure of sequence from Rattus norvegicus with DHT as ligand. Full crystallographic information is available from OCA.
Reference
Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone., Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, Wu GY, Scheffler JE, Salvati ME, Krystek SR Jr, Weinmann R, Einspahr HM, Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):4904-9. PMID:11320241
Page seeded by OCA on Tue Nov 20 17:01:22 2007
