Article
Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone.
Proceedings of the National Academy of Sciences of the United States of America - 24 Apr 2001
Sack J S, Kish K F, Wang C, Attar R M, Kiefer S E, An Y, Wu G Y, Scheffler J E, Salvati M E, Krystek S R, Weinmann R, Einspahr H M
Abstract excerpt
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...
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