4UQJ

Cryo-EM density map of GluA2em in complex with ZK200775

4UQJ の概要

• エントリーDOI: 10.2210/pdb4uqj/pdb
• 関連するPDBエントリー: 4UQ6 4UQK 4UQQ
• EMDBエントリー: 2680
• 分子名称: GLUTAMATE RECEPTOR 2, {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid (2 entities in total)
• 機能のキーワード: transport protein, glua2em antagonist-bound closed state
• 由来する生物種: RATTUS NORVEGICUS (NORWAY RAT)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P19491
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 371731.48

構造登録者

Meyerson, J.R.,Kumar, J.,Chittori, S.,Rao, P.,Pierson, J.,Bartesaghi, A.,Mayer, M.L.,Subramaniam, S. (登録日: 2014-06-24, 公開日: 2014-08-13, 最終更新日: 2024-11-13)

主引用文献

Meyerson, J.R.,Kumar, J.,Chittori, S.,Rao, P.,Pierson, J.,Bartesaghi, A.,Mayer, M.L.,Subramaniam, S.
Structural Mechanism of Glutamate Receptor Activation and Desensitization
Nature, 514:328-, 2014

PubMed Abstract: Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion flux across the membrane, we trapped rat AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) and kainate receptor subtypes in their major functional states and analysed the resulting structures using cryo-electron microscopy. We show that transition to the active state involves a 'corkscrew' motion of the receptor assembly, driven by closure of the ligand-binding domain. Desensitization is accompanied by disruption of the amino-terminal domain tetramer in AMPA, but not kainate, receptors with a two-fold to four-fold symmetry transition in the ligand-binding domains in both subtypes. The 7.6 Å structure of a desensitized kainate receptor shows how these changes accommodate channel closing. These findings integrate previous physiological, biochemical and structural analyses of glutamate receptors and provide a molecular explanation for key steps in receptor gating.

PubMed: 25119039
DOI: 10.1038/NATURE13603

実験手法

ELECTRON MICROSCOPY (10.4 Å)