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

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.

SUBMITTER: Jin R

PROVIDER: S-EPMC2699365 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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

Jin Rongsheng R Singh Satinder K SK Gu Shenyan S Furukawa Hiroyasu H Sobolevsky Alexander I AI Zhou Jie J Jin Yan Y Gouaux Eric E

The EMBO journal 20090521 12

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 b ...[more]

PMID: 19461580

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