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Calmodulin regulates human ether à go-go 1 (hEAG1) potassium channels through interactions of the Eag domain with the cyclic nucleotide binding homology domain.

Abstract:

The ether à go-go family of voltage-gated potassium channels is structurally distinct. The N terminus contains an eag domain (eagD) that contains a Per-Arnt-Sim (PAS) domain that is preceded by a conserved sequence of 25-27 amino acids known as the PAS-cap. The C terminus contains a region with homology to cyclic nucleotide binding domains (cNBHD), which is directly linked to the channel pore. The human EAG1 (hEAG1) channel is remarkably sensitive to inhibition by intracellular calcium (Ca(2+...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1074/jbc.m116.733576

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
ORCID:
0000-0001-8800-7669
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Publisher:
American Society for Biochemistry and Molecular Biology Publisher's website
Journal:
Journal of Biological Chemistry Journal website
Volume:
291
Issue:
34
Pages:
17907-17918
Publication date:
2016-06-01
Acceptance date:
2016-05-27
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pmid:
27325704
Source identifiers:
630020
Language:
English
Keywords:
Pubs id:
pubs:630020
UUID:
uuid:8d59e69b-5a92-4af8-bfd1-9969e750f513
Local pid:
pubs:630020
Deposit date:
2018-03-13

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