Crystal Structure of the GluR2 Amino-Terminal Domain Provides Insights into the Architecture and Assembly of Ionotropic Glutamate Receptors
- Resource Type
- Article
- Authors
- Clayton, Amber; Siebold, Christian; Gilbert, Robert J.C.; Sutton, Geoffrey C.; Harlos, Karl; McIlhinney, R. A. Jeffrey; Jones, E. Yvonne; Aricescu, A. Radu
- Source
- Journal of Molecular Biology. Oct2009, Vol. 392 Issue 5, p1125-1132. 8p.
- Subject
- *AMINO acid sequence
*STRUCTURE-activity relationships in cell receptors
*CRYSTALLOGRAPHY
*GLUTAMIC acid
*CELL receptors
*PROPIONIC acid
*CARRIER proteins
*CRYSTAL lattices
*ELECTRON microscopy
- Language
- ISSN
- 0022-2836
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. [Copyright &y& Elsevier]