Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2186265 | Journal of Molecular Biology | 2009 | 8 Pages |
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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Authors
Amber Clayton, Christian Siebold, Robert J.C. Gilbert, Geoffrey C. Sutton, Karl Harlos, R. A. Jeffrey McIlhinney, E. Yvonne Jones, A. Radu Aricescu,