2GFE

Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution

2GFE の概要

• エントリーDOI: 10.2210/pdb2gfe/pdb
• 関連するPDBエントリー: 1FTJ 1S50 2F36
• 分子名称: Glutamate receptor 2, ZINC ION, GLUTAMIC ACID, ... (4 entities in total)
• 機能のキーワード: 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: 3
• 化学式量合計: 88430.39

構造登録者

Mayer, M.L. (登録日: 2006-03-21, 公開日: 2006-08-22, 最終更新日: 2024-11-20)

主引用文献

Weston, M.C.,Gertler, C.,Mayer, M.L.,Rosenmund, C.
Interdomain interactions in AMPA and kainate receptors regulate affinity for glutamate.
J.Neurosci., 26:7650-7658, 2006

PubMed Abstract: Ionotropic glutamate receptors perform diverse functions in the nervous system. As a result, multiple receptor subtypes have evolved with different kinetics, ion permeability, expression patterns, and regulation by second messengers. Kainate receptors show slower recovery from desensitization and have different affinities for agonists than AMPA receptors. Based on analysis of ligand binding domain crystal structures, we identified interdomain interactions in the agonist-bound state that are conserved in kainate receptors and absent in AMPA receptors. Mutations in GluR6 designed to disrupt these contacts reduced agonist apparent affinity, speeded up receptor deactivation and increased the rate of recovery from desensitization. Conversely, introduction of mutations in GluR2 that enabled additional interdomain interactions in the agonist-bound state increased agonist apparent affinity 15-fold, and slowed both deactivation and recovery from desensitization. We conclude that interdomain interactions have evolved as a distinct mechanism that contributes to the unique kinetic properties of AMPA and kainate receptors.

PubMed: 16855092
DOI: 10.1523/JNEUROSCI.1519-06.2006

実験手法

X-RAY DIFFRACTION (1.54 Å)