- Abstract:
-
Desensitization is an important mechanism curtailing the activity of ligand-gated ion channels (LGICs). Although the structural basis of desensitization is not fully resolved, it is thought to be governed by physicochemical properties of bound ligands. Here, we show the importance of an allosteric cation-binding pocket in controlling transitions between activated and desensitized states of rat kainate-type (KAR) ionotropic glutamate receptors (iGluRs). Tethering a positive charge to this pock...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1038/nsmb.2654
-
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- Journal:
- Nature structural and molecular biology
- Volume:
- 20
- Issue:
- 9
- Pages:
- 1054-1061
- Publication date:
- 2013-09-05
- DOI:
- EISSN:
-
1545-9985
- ISSN:
-
1545-9993
- URN:
-
uuid:798949c7-8690-4957-8ca6-617e209c65f4
- Source identifiers:
-
418507
- Local pid:
- pubs:418507
- Copyright date:
- 2013
Journal article
Defining the structural relationship between kainate-receptor deactivation and desensitization.
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