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)
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 |
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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: | https://repository.cshl.edu/id/eprint/25162 |
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