1I37

CRYSTAL STRUCTURE OF THE RAT ANDROGEN RECEPTOR LIGAND BINDING DOMAIN COMPLEX WITH DIHYDROTESTOSTERONE

1I37 の概要

• エントリーDOI: 10.2210/pdb1i37/pdb
• 関連するPDBエントリー: 1I38
• 分子名称: ANDROGEN RECEPTOR, 5-ALPHA-DIHYDROTESTOSTERONE (3 entities in total)
• 機能のキーワード: androgen receptor, steroid receptor, nuclear receptor, transcription regulation, ligand-binding domain, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: P15207
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30572.85

構造登録者

Sack, J.S. (登録日: 2001-02-13, 公開日: 2001-03-21, 最終更新日: 2023-08-09)

主引用文献

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

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: 11320241
DOI: 10.1073/pnas.081565498

実験手法

X-RAY DIFFRACTION (2 Å)