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Defining the structural relationship between kainate-receptor deactivation and desensitization.

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...

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Publication status:
Published

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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

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