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

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

Amber Clayton  1 , Christian Siebold, Robert J C Gilbert, Geoffrey C Sutton, Karl Harlos, R A Jeffrey McIlhinney, E Yvonne Jones, A Radu Aricescu
Affiliations

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

Amber Clayton et al. J Mol Biol. .

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.

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