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A specific two-pore domain potassium channel blocker defines the structure of the TASK-1 open pore.

Abstract:

Two-pore domain potassium (K(2P)) channels play a key role in setting the membrane potential of excitable cells. Despite their role as putative targets for drugs and general anesthetics, little is known about the structure and the drug binding site of K(2P) channels. We describe A1899 as a potent and highly selective blocker of the K(2P) channel TASK-1. As A1899 acts as an open-channel blocker and binds to residues forming the wall of the central cavity, the drug was used to further our under...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m111.227884

Authors


Streit, AK More by this author
Netter, MF More by this author
Walecki, M More by this author
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Journal:
The Journal of biological chemistry
Volume:
286
Issue:
16
Pages:
13977-13984
Publication date:
2011-04-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:9e33b704-3829-48e9-8044-a3099037e815
Source identifiers:
135155
Local pid:
pubs:135155

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