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

Published on 05.21.2009 in The EMBO Journal

Authors:

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

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.