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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-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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.jmb.2009.07.082

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
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Funding agency for:
Siebold, C
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Funding agency for:
Gilbert, R
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Funding agency for:
Aricescu, A
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Funding agency for:
Jones, E
Medical Research Council More from this funder
Publisher:
Elsevier Publisher's website
Journal:
Journal of Molecular Biology Journal website
Volume:
392
Issue:
5
Pages:
1125-1132
Publication date:
2009-10-01
DOI:
ISSN:
0022-2836
Language:
English
Keywords:
Subjects:
UUID:
uuid:5d4392b9-f2dc-4e83-9880-788c003d15a8
Local pid:
ora:4328
Deposit date:
2010-10-28

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