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. (June 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) (Public Dataset)

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: 17 June 2009
Date Deposited: 26 Mar 2012 17:58
Last Modified: 08 Sep 2017 16:05
PMCID: PMC2699365
Related URLs:
Dataset ID:
URI: http://repository.cshl.edu/id/eprint/25162

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