Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone

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 Å resolution. In contrast to the homodimer seen in the retinoid-X receptor and estrogen re...

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Hlavní autoři: Sack, John S., Kish, Kevin F., Wang, Chihuei, Attar, Ricardo M., Kiefer, Susan E., An, Yongmi, Wu, Ginger Y., Scheffler, Julie E., Salvati, Mark E., Krystek, Stanley R., Weinmann, Roberto, Einspahr, Howard M.
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 2001
Témata:
Biological Sciences
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC33136/
https://ncbi.nlm.nih.gov/pubmed/11320241
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.081565498
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