- 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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1016/j.bpj.2017.08.047
-
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- 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
- Copyright holder:
- Biophysical Society
- Copyright date:
- 2017
- Notes:
- © 2017 Biophysical Society.
Journal article
Functional validation of Heteromeric Kainate receptor models
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