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

Publication Type:

Journal Article


EMBO J, Volume 28, Issue 12, p.1812-23 (2009)


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, Rats, Receptors, AMPA, Solutions


<p>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.</p>