1GR2

STRUCTURE OF A GLUTAMATE RECEPTOR LIGAND BINDING CORE (GLUR2) COMPLEXED WITH KAINATE

1GR2 の概要

• エントリーDOI: 10.2210/pdb1gr2/pdb
• 分子名称: PROTEIN (GLUTAMATE RECEPTOR 2), 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE (3 entities in total)
• 機能のキーワード: excitory neurotransmitter receptor, glutamate receptor, 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: 30954.43

構造登録者

Armstrong, N.,Sun, Y.,Chen, G.Q.,Gouaux, E. (登録日: 1998-09-17, 公開日: 1998-12-09, 最終更新日: 2024-10-16)

主引用文献

Armstrong, N.,Sun, Y.,Chen, G.Q.,Gouaux, E.
Structure of a glutamate-receptor ligand-binding core in complex with kainate.
Nature, 395:913-917, 1998

PubMed Abstract: Ionotropic glutamate receptors (iGluRs) mediate excitatory synaptic transmission in vertebrates and invertebrates through ligand-induced opening of transmembrane ion channels. iGluRs are segregated into three subtypes according to their sensitivity to the agonists AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid), kainate (a structural analogue of glutamate) or NMDA (N-methyl-D-aspartate). iGluRs are important in the development and function of the nervous system, are essential in memory and learning, and are either implicated in or have causal roles in dysfunctions ranging from Alzheimer's, Parkinson's and Huntington's diseases, schizophrenia, epilepsy and Rasmussen's encephalitis to stroke. Development of iGluR agonists and antagonists has been hampered by a lack of high-resolution structural information. Here we describe the crystal structure of an iGluR ligand-binding region in a complex with the neurotoxin (agonist) kainate. The bilobed structure shows the determinants of receptor-agonist interactions and how ligand-binding specificity and affinity are altered by remote residues and the redox state of the conserved disulphide bond. The structure indicates mechanisms for allosteric effector action and for ligand-induced channel gating. The information provided by this structure will be essential in designing new ligands.

PubMed: 9804426
DOI: 10.1038/27692

実験手法

X-RAY DIFFRACTION (1.9 Å)