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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.

Original publication

DOI

10.1016/j.jmb.2009.07.082

Type

Journal article

Journal

J Mol Biol

Publication Date

09/10/2009

Volume

392

Pages

1125 - 1132

Keywords

Crystallography, X-Ray, Humans, Models, Molecular, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Receptors, AMPA