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

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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*
  • Receptors, AMPA / metabolism*
  • Solutions

Substances

  • Amino Acids
  • Protein Subunits
  • Receptors, AMPA
  • Solutions
  • glutamate receptor ionotropic, AMPA 2

Associated data

  • PDB/3H5V
  • PDB/3H5W