Journal article icon

Journal article

Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.

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

Actions


Access Document


Publisher copy:
10.1016/j.jmb.2009.07.082

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Expand authors...
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

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP