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Functional validation of Heteromeric Kainate receptor models

Abstract:

Kainate receptors require the presence of external ions for gating. Most work thus far has been performed on homomeric GluK2 but, in vivo, kainate receptors are likely heterotetramers. Agonists bind to the ligand-binding domain (LBD) which is arranged as a dimer of dimers as exemplified in homomeric structures, but no high-resolution structure currently exists of heteromeric kainate receptors. In a full-length heterotetramer, the LBDs could potentially be arranged either as a GluK2 homomer al...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.bpj.2017.08.047

Authors


More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
ORCID:
0000-0001-6096-9014
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Oxford college:
Lady Margaret Hall; Lady Margaret Hall
Role:
Author
ORCID:
0000-0001-5100-8836
Publisher:
Cell Press Publisher's website
Journal:
Biophysical Journal Journal website
Volume:
113
Issue:
10
Pages:
2173-2177
Publication date:
2017-09-19
Acceptance date:
2017-08-31
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
Pubs id:
pubs:731042
URN:
uri:8dccf7c4-8571-4c72-9fc8-3326455e7ba9
UUID:
uuid:8dccf7c4-8571-4c72-9fc8-3326455e7ba9
Local pid:
pubs:731042
Language:
English

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