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The pore structure and gating mechanism of K2P channels

Abstract:

Two-pore domain (K2P) potassium channels are important regulators of cellular electrical excitability. However, the structure of these channels and their gating mechanism, in particular the role of the bundle-crossing gate, are not well understood. Here, we report that quaternary ammonium (QA) ions bind with high-affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure. This demonstrates that, unlike most othe...

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Publisher copy:
10.1038/emboj.2011.268

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Journal:
EMBO Journal
Volume:
30
Issue:
17
Pages:
3607-3619
Publication date:
2011-08-31
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
Source identifiers:
179646
Language:
English
Keywords:
Pubs id:
pubs:179646
UUID:
uuid:c3a5c5a4-fb10-45a7-8d43-2d2259a1ed46
Local pid:
pubs:179646
Deposit date:
2012-12-19

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