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Cited by 214Ion channel regulation and functionProtein Structure and DynamicsCardiac electrophysiology and arrhythmias

A gate in the selectivity filter of potassium channels

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Bernèche, Simon, Roux, Benoît·2005·Structure
DOI 10.1016/j.str.2004.12.019
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Abstract

The selectivity filter of potassium channels is the structural element directly responsible for the selective and rapid conduction of K+, whereas other parts of the protein are thought to function as a molecular gate that either permits or blocks the passage of ions. However, whether the selectivity filter itself also possesses the ability to play the role of a gate is an unresolved question. Using free energy molecular dynamics simulations, it is shown that the reorientation of two peptide linkages in the selectivity filter of the KcsA K+ channel can lead to a stable nonconducting conformational state. Two microscopic factors influence the transition toward such a conformational state: the occupancy of one specific cation binding site in the selectivity filter (S2), and the strength of intersubunit interactions involving the GYG signature sequence. These results suggest that such conformational transitions occurring in the selectivity filter might be related to different K+ channel gating events, including C-type (slow) inactivation.

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Crossref · 10.1016/j.str.2004.12.019

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  • Changes between a non-conductive and a conductive state in KcsA occur at a rate of 7.1 × 103 s−1, giving a life-time of the non-conducting state of 0.14 ms.

    “Changes between a non-conductive and a conductive state in the KcsA occur at a rate of 7.1 × 103 s−1, giving a life-time of the non-conducting state of 0.14 ms (~10−4 s) [89].”

    From An Overview of Sub-Cellular Mechanisms Involved in the Action of TTFields (2016) · cites this paper as [89]

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Authors
Bernèche, S., & Roux, B.
Affiliations
Cornell University (US)
Corresponding author
Bernèche, Simon
ORCID
Bernèche, Simon
Venue
Structure
Publisher
Elsevier BV
Published
2005-04
Volume
13
Issue
4
Pages
591-600
ISSN
0969-2126 (ISSN-L)
DOI
10.1016/j.str.2004.12.019
OpenAlex
W2117055264
Cited by
214
References
71
Citations by year
2026: 3 · 2025: 3 · 2024: 12 · 2023: 2 · 2022: 4 · 2021: 8 · 2020: 8 · 2019: 4 · 2018: 12 · 2017: 5 · 2016: 6 · 2015: 5 · 2014: 7 · 2013: 10 · 2012: 15
FWCI
7.85
Type
journal article
Language
en
Open access
Licence
Locations
  • Structure (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
Keywords
KcsA, ion selectivity, cation binding sites, intersubunit interactions, C-type inactivation, channel gating
MeSH terms
Protein Conformation, Potassium Channels, Ion Channel Gating

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