ArticleProceedings of the National Academy of Sciences of the United States of America2011
Mechanism for selectivity-inactivation coupling in KcsA potassium channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- From Selective Permeation to Physiology in Potassium Channels.Function (Oxford, England) · 2025Review
- Elucidating the role of lipid interactions in stabilizing the membrane protein KcsA.Biophysical journal · 2024Article
- Potassium dependent structural changes in the selectivity filter of HERG potassium channels.Nature communications · 2024Article
- Article
- Interactions between selectivity filter and pore helix control filter gating in the MthK channel.The Journal of general physiology · 2023Article
- Article
- Article
- Molecular Events behind the Selectivity and Inactivation Properties of Model NaK-Derived Ion Channels.International journal of molecular sciences · 2022Article
- Structural Basis for pH-gating of the KNature communications · 2022Article
- Article
- Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel.Nature communications · 2021Article
- Pore-forming transmembrane domains control ion selectivity and selectivity filter conformation in the KirBac1.1 potassium channel.The Journal of general physiology · 2021Article
- Regulation of KMembranes · 2021Article
- Review
- Unraveling of a Strongly Correlated Dynamical Network of Residues Controlling the Permeation of Potassium in KcsA Ion Channel.Entropy (Basel, Switzerland) · 2021Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- Structural Plasticity of the Selectivity Filter in Cation Channels.Frontiers in physiology · 2021Review
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- Molecular Insights Into the Gating Kinetics of the Cardiac hERG Channel, Illuminated by Structure and Molecular Dynamics.Frontiers in pharmacology · 2021Review
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5 authors.
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Abstract
Structures of the prokaryotic K(+) channel, KcsA, highlight the role of the selectivity filter carbonyls from the GYG signature sequence in determining a highly selective pore, but channels displaying this sequence vary widely in their cation selectivity. Furthermore, variable selectivity can be found within the same channel during a process called C-type inactivation. We investigated the mechanism for changes in selectivity associated with inactivation in a model K(+) channel, KcsA. We found that E71A, a noninactivating KcsA mutant in which a hydrogen-bond behind the selectivity filter is disrupted, also displays decreased K(+) selectivity. In E71A channels, Na(+) permeates at higher rates as seen with and flux measurements and analysis of intracellular Na(+) block. Crystal structures of E71A reveal that the selectivity filter no longer assumes the "collapsed," presumed inactivated, conformation in low K(+), but a "flipped" conformation, that is also observed in high K(+), high Na(+), and even Na(+) only conditions. The data reveal the importance of the E71-D80 interaction in both favoring inactivation and maintaining high K(+) selectivity. We propose a molecular mechanism by which inactivation and K(+) selectivity are linked, a mechanism that may also be at work in other channels containing the canonical GYG signature sequence.
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