Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors

J Mol Biol. 2009 Oct 9;392(5):1125-32. doi: 10.1016/j.jmb.2009.07.082. Epub 2009 Aug 3.

Abstract

Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-A resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-A resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic data for full-length AMPA receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Receptors, AMPA / chemistry*

Substances

  • Receptors, AMPA
  • glutamate receptor ionotropic, AMPA 2

Associated data

  • PDB/2WJW
  • PDB/2WJX