- Abstract:
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Several recent ion channel structures have revealed large side portals, or ‘fenestrations’ at the interface between their transmembrane helices that potentially expose the ion conduction pathway to the lipid core of the bilayer. In a recent study we demonstrated that functional activity of the TWIK-1 K2P channel is influenced by the presence of hydrophobic residues deep within the inner pore. These residues are located near the fenestrations in the TWIK-1 structure and promote dewetting of th...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 652.4KB)
-
- Publisher copy:
- 10.4161/19336950.2014.981987
-
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- Publisher:
- Taylor and Francis Publisher's website
- Journal:
- Channels Journal website
- Volume:
- 9
- Issue:
- 1
- Pages:
- 44-49
- Publication date:
- 2014-10-24
- DOI:
- EISSN:
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1933-6969
- ISSN:
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1933-6969
- URN:
-
uuid:39b00288-a5fc-41a2-8187-7952a0c43fc1
- Source identifiers:
-
492139
- Local pid:
- pubs:492139
- Language:
- English
- Keywords:
- Copyright holder:
- Aryal et al.
- Copyright date:
- 2014
- Notes:
-
Copyright © 2015 The Author(s). Published with license by Taylor and Francis Group, LLC© Prafulla Aryal, Firdaus Abd-Wahab, Giovanna Bucci, Mark SP Sansom, and Stephen J Tucker
This is an Open Access article distributed under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
Journal article
Influence of lipids on the hydrophobic barrier within the pore of the TWIK-1 K2P channel
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Pfizer Neusentis
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