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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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| Main Authors: | , , , , , , , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
The National Academy of Sciences
2001
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| Fag: | |
| Online adgang: | 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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