Article ID Journal Published Year Pages File Type
2186265 Journal of Molecular Biology 2009 8 Pages PDF
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-Å 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-Å 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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