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

Journal Article · Wed Sep 02 04:00:00 EDT 2009 · EMBO J.

DOI:https://doi.org/10.1038/emboj.2009.140· OSTI ID:1005776

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

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.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: USDOE
• OSTI ID: 1005776
• Journal Information: EMBO J., Journal Name: EMBO J. Journal Issue: (12) ; 06, 2009 Vol. 28; ISSN EMJODG; ISSN 0261-4189
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
ARCHITECTURE
CRYSTAL STRUCTURE
CRYSTALLOGRAPHY
DIMERS
PROTEINS