1X7R

CRYSTAL STRUCTURE OF ESTROGEN RECEPTOR ALPHA COMPLEXED WITH GENISTEIN

1X7R の概要

• エントリーDOI: 10.2210/pdb1x7r/pdb
• 関連するPDBエントリー: 1U3Q 1U3R 1U3S 1U9E 1X76 1X78 1X7B 1X7J
• 分子名称: Estrogen receptor 1 (alpha), steroid receptor coactivator-3, GENISTEIN, ... (4 entities in total)
• 機能のキーワード: estrogen receptor, estrogen receptor beta, er-beta, er, estrogen receptor alpha, er-alpha, estrogen, nuclear recept transcription factor, agonist, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Isoform 1: Nucleus. Isoform 3: Nucleus: P03372
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29914.22

構造登録者

Manas, E.S.,Xu, Z.B.,Unwalla, R.J.,Somers, W.S. (登録日: 2004-08-16, 公開日: 2005-03-01, 最終更新日: 2024-04-03)

主引用文献

Manas, E.S.,Xu, Z.B.,Unwalla, R.J.,Somers, W.S.
Understanding the Selectivity of Genistein for Human Estrogen Receptor-Beta Using X-Ray Crystallography and Computational Methods
Structure, 12:2197-2207, 2004

PubMed Abstract: We present X-ray crystallographic and molecular modeling studies of estrogen receptors-alpha and -beta complexed with the estrogen receptor-beta-selective phytoestrogen genistein, and coactivator-derived NR box peptides containing an LXXLL motif. We demonstrate that the ligand binding mode is essentially identical when genistein is bound to both isoforms, despite the considerably weaker affinity of this ligand for estrogen receptor-alpha. In addition, we examine subtle differences between binding site residues, providing an explanation for why genistein is modestly selective for the beta isoform. To this end, we also present the results of quantum chemical studies and thermodynamic arguments that yield insight to the nature of the interactions leading to estrogen receptor-beta selectivity. The importance of our analysis to structure-based drug design is discussed.

PubMed: 15576033
DOI: 10.1016/j.str.2004.09.015

実験手法

X-RAY DIFFRACTION (2 Å)