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EMBO J. 2009 Jun 17;28(12):1812-23. doi: 10.1038/emboj.2009.140. Epub 2009 May 21.

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

Author information

1
Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, La Jolla, CA, USA. rjin@burnham.org

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.

PMID:
19461580
PMCID:
PMC2699365
DOI:
10.1038/emboj.2009.140
[Indexed for MEDLINE]
Free PMC Article
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