Crystal structure and association behaviour of the GluR2 amino-terminal domain

Jin, R., Singh, S. K., Gu, S., Furukawa, H., Sobolevsky, A. I., Zhou, J., Jin, Y., Gouaux, E. (2009) Crystal structure and association behaviour of the GluR2 amino-terminal domain. Embo J, 28 (12). pp. 1812-23. ISSN 1460-2075 (Electronic)1460-2075 (Linking)

URL: https://www.ncbi.nlm.nih.gov/pubmed/19461580
DOI: 10.1038/emboj.2009.140

Abstract

Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Amino Acids Animals Binding Sites Cell Line Conserved Sequence Crystallography X-Ray Models Molecular Molecular Sequence Data Protein Binding Protein Conformation Protein Multimerization Protein Stability Protein Structure Tertiary Protein Subunits chemistry Rats Receptors, AMPA chemistry metabolism Solutions
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > AMPA receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > ionotropic glutamate receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
CSHL Authors:
Communities: CSHL labs > Furukawa lab
Depositing User: Leigh Johnson
Date Deposited: 26 Mar 2012 17:58
Last Modified: 08 Sep 2017 16:05
PMCID: PMC2699365
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Dataset ID:
URI: http://repository.cshl.edu/id/eprint/25162

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