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

Rongsheng Jin, Satinder K. Singh, Shenyan Gu, Hiroyasu Furukawa, Alexander I. Sobolevsky, Jie Zhou, Yan Jin, Eric Gouaux

Research output: Contribution to journalArticle

123 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1812-1823
Number of pages12
JournalEMBO Journal
Volume28
Issue number12
DOIs
StatePublished - Jun 17 2009

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Keywords

  • Amino-terminal domain
  • GluR2
  • Glutamate receptor
  • Ion channel
  • X-ray crystallography

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

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 Journal, 28(12), 1812-1823. https://doi.org/10.1038/emboj.2009.140