3H5V

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

(2009) EMBO J 28: 1812-1823

• PubMed: 19461580 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/emboj.2009.140
• Primary Citation of Related Structures:  
  3H5V, 3H5W


• PubMed 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.

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Organizational Affiliation: 

Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, La Jolla, CA, USA. [email protected]