1FTO

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE AT 2.0 A RESOLUTION

1FTO の概要

• エントリーDOI: 10.2210/pdb1fto/pdb
• 関連するPDBエントリー: 1FTJ 1FTK 1FTL 1FTM 1FW0 1GR2
• 分子名称: GLUTAMATE RECEPTOR SUBUNIT 2 (2 entities in total)
• 機能のキーワード: ionotropic glutamate receptor, unligandeded, apo, ligand binding domain, 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: 2
• 化学式量合計: 58443.36

構造登録者

Armstrong, N.,Gouaux, E. (登録日: 2000-09-12, 公開日: 2000-11-01, 最終更新日: 2024-11-06)

主引用文献

Armstrong, N.,Gouaux, E.
Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core.
Neuron, 28:165-181, 2000

PubMed Abstract: Crystal structures of the GluR2 ligand binding core (S1S2) have been determined in the apo state and in the presence of the antagonist DNQX, the partial agonist kainate, and the full agonists AMPA and glutamate. The domains of the S1S2 ligand binding core are expanded in the apo state and contract upon ligand binding with the extent of domain separation decreasing in the order of apo > DNQX > kainate > glutamate approximately equal to AMPA. These results suggest that agonist-induced domain closure gates the transmembrane channel and the extent of receptor activation depends upon the degree of domain closure. AMPA and glutamate also promote a 180 degrees flip of a trans peptide bond in the ligand binding site. The crystal packing of the ligand binding cores suggests modes for subunit-subunit contact in the intact receptor and mechanisms by which allosteric effectors modulate receptor activity.

PubMed: 11086992
DOI: 10.1016/S0896-6273(00)00094-5

実験手法

X-RAY DIFFRACTION (2 Å)