1I37
CRYSTAL STRUCTURE OF THE RAT ANDROGEN RECEPTOR LIGAND BINDING DOMAIN COMPLEX WITH DIHYDROTESTOSTERONE
Summary for 1I37
| Entry DOI | 10.2210/pdb1i37/pdb |
| Related | 1I38 |
| Descriptor | ANDROGEN RECEPTOR, 5-ALPHA-DIHYDROTESTOSTERONE (3 entities in total) |
| Functional Keywords | androgen receptor, steroid receptor, nuclear receptor, transcription regulation, ligand-binding domain, hormone-growth factor complex, hormone/growth factor |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Nucleus: P15207 |
| Total number of polymer chains | 1 |
| Total formula weight | 30572.85 |
| Authors | Sack, J.S. (deposition date: 2001-02-13, release date: 2001-03-21, Last modification date: 2023-08-09) |
| Primary citation | 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 Jr., S.R.,Weinmann, R.,Einspahr, H.M. Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone. Proc.Natl.Acad.Sci.USA, 98:4904-4909, 2001 Cited by PubMed Abstract: 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. PubMed: 11320241DOI: 10.1073/pnas.081565498 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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