1MQH

Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Bromo-Willardiine at 1.8 Angstroms Resolution

1MQH の概要

• エントリーDOI: 10.2210/pdb1mqh/pdb
• 関連するPDBエントリー: 1FTJ 1FTM 1MM6 1MM7 1MQG 1MQI 1MQJ
• 分子名称: glutamate receptor 2, 2-AMINO-3-(5-BROMO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID (3 entities in total)
• 機能のキーワード: ionotropic glutamate receptor, glur2, ligand binding core, s1s2, partial agonist, willardiines, bromo-willardiine, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P19491
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29439.62

構造登録者

Jin, R.,Banke, T.G.,Mayer, M.L.,Traynelis, S.F.,Gouaux, E. (登録日: 2002-09-16, 公開日: 2003-08-05, 最終更新日: 2024-11-13)

主引用文献

Jin, R.,Banke, T.G.,Mayer, M.L.,Traynelis, S.F.,Gouaux, E.
Structural basis for partial agonist action at ionotropic glutamate receptors
Nat.Neurosci., 6:803-810, 2003

PubMed Abstract: An unresolved problem in understanding neurotransmitter receptor function concerns the mechanism(s) by which full and partial agonists elicit different amplitude responses at equal receptor occupancy. The widely held view of 'partial agonism' posits that resting and active states of the receptor are in equilibrium, and partial agonists simply do not shift the equilibrium toward the active state as efficaciously as full agonists. Here we report findings from crystallographic and electrophysiological studies of the mechanism of activation of an AMPA-subtype glutamate receptor ion channel. In these experiments, we used 5-substituted willardiines, a series of partial agonists that differ by only a single atom. Our results show that the GluR2 ligand-binding core can adopt a range of ligand-dependent conformational states, which in turn control the open probability of discrete subconductance states of the intact ion channel. Our findings thus provide a structure-based model of partial agonism.

PubMed: 12872125
DOI: 10.1038/nn1091

実験手法

X-RAY DIFFRACTION (1.8 Å)