Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors
| Autor: | Christian Siebold, A. Radu Aricescu, Amber J. Clayton, E. Yvonne Jones, Robert J.C. Gilbert, Geoffrey C. Sutton, R. A. Jeffrey McIlhinney, Karl Harlos |
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| Rok vydání: | 2009 |
| Předmět: |
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Molecular Stereochemistry Chemistry Genetics (medical sciences) Glutamate receptor AMPA receptor Crystal structure Crystallography X-Ray Protein Structure Tertiary Protein structure Structural Biology NMDA receptor Humans Receptors AMPA Protein Multimerization Receptor Protein Structure Quaternary Molecular Biology Ion channel Ionotropic effect |
| Zdroj: | Journal of molecular biology. 392(5) |
| ISSN: | 1089-8638 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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