- 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-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.
- Publication status:
- Published
- Publisher copy:
- 10.1016/j.jmb.2009.07.082
-
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- Journal:
- Journal of molecular biology
- Volume:
- 392
- Issue:
- 5
- Pages:
- 1125-1132
- Publication date:
- 2009-10-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:69e8f918-332d-49f3-afc9-1593b6de2fa7
- Source identifiers:
-
22347
- Local pid:
- pubs:22347
- Copyright date:
- 2009
Journal article
Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.
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