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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
Version:
Publisher's version

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Publisher copy:
10.1074/jbc.m116.733576

Authors


Lörinczi, E More by this author
Helliwell, M More by this author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
ORCID:
0000-0001-8800-7669
Davies, NW More by this author
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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:
2016-06-05
Acceptance date:
2016-05-27
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pubs id:
pubs:630020
URN:
uri:8d59e69b-5a92-4af8-bfd1-9969e750f513
UUID:
uuid:8d59e69b-5a92-4af8-bfd1-9969e750f513
Local pid:
pubs:630020

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