Crystal Structure of the GluR2 Amino-Terminal Domain Provides Insights into the Architecture and Assembly of Ionotropic Glutamate Receptors

被引：65

作者：

Clayton, Amber ^{[1
]}

Siebold, Christian ^{[1
]}

Gilbert, Robert J. C. ^{[1
]}

Sutton, Geoffrey C. ^{[1
]}

Harlos, Karl ^{[1
]}

McIlhinney, R. A. Jeffrey ^{[2
]}

Jones, E. Yvonne ^{[1
]}

Aricescu, A. Radu ^{[1
]}

机构：

[1] Univ Oxford, Div Struct Biol, Wellcome Trust Ctr Human Genet, Oxford OX3 7BN, England

[2] MRC, Anat Neuropharmacol Unit, Oxford OX1 3TH, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2009年 / 392卷 / 05期

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

ion channel; glutamate receptor; synaptic plasticity; cell surface receptor; crystal structure; LIGAND-BINDING PROPERTIES; AMPA RECEPTOR; SYNAPTIC PLASTICITY; ION CHANNELS; 3-DIMENSIONAL STRUCTURE; QUATERNARY STRUCTURE; SUBUNIT; OLIGOMERIZATION; MECHANISM; DIMERS;

D O I：

10.1016/j.jmb.2009.07.082

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-angstrom resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-angstrom resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic data for full-length AMPA receptors. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：1125 / 1132

页数：8

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