ArticleBiophysical journal2011
3₁₀-helix conformation facilitates the transition of a voltage sensor S4 segment toward the down state.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Infrared photons generated by voltage-gated sodium channel dynamics: a hypothesis for cooperative electrodynamic interactions at the axon initial segment.Frontiers in human neuroscience · 2026Review
- AlphaFold2 captures conformational transitions in the voltage-gated channel superfamily.Biophysical journal · 2025Article
- Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP.Nature communications · 2024Article
- Non-canonical helical transitions and conformational switching are associated with characteristic flexibility and disorder indices in TRP and Kv channels.Channels (Austin, Tex.) · 2023Article
- The 70-year search for the voltage-sensing mechanism of ion channels.The Journal of physiology · 2022Article
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- Aberrant Expression of a Non-muscle RBFOX2 Isoform Triggers Cardiac Conduction Defects in Myotonic Dystrophy.Developmental cell · 2020Article
- Molecular Insights from Conformational Ensembles via Machine Learning.Biophysical journal · 2020Article
- The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix.Frontiers in molecular biosciences · 2020Article
- Voltage-dependent gating in K channels: experimental results and quantitative models.Pflugers Archiv : European journal of physiology · 2020Review
- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Simulation of Gating Currents of the Shaker K Channel Using a Brownian Model of the Voltage Sensor.Biophysical journal · 2019Article
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Challenges and advances in atomistic simulations of potassium and sodium ion channel gating and permeation.The Journal of physiology · 2019Review
- Main-chain mutagenesis reveals intrahelical coupling in an ion channel voltage-sensor.Nature communications · 2018Article
- Does Proton Conduction in the Voltage-Gated HThe journal of physical chemistry. B · 2017Article
- Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels.Scientific reports · 2016Article
- Cardiac Na Channels: Structure to Function.Current topics in membranes · 2016Article
- Voltage sensor gating charge transfer in a hERG potassium channel model.Biophysical journal · 2014Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The activation of voltage-gated ion channels is controlled by the S4 helix, with arginines every third residue. The x-ray structures are believed to reflect an open-inactivated state, and models propose combinations of translation, rotation, and tilt to reach the resting state. Recently, experiments and simulations have independently observed occurrence of 3(10)-helix in S4. This suggests S4 might make a transition from α- to 3(10)-helix in the gating process. Here, we show 3(10)-helix structure between Q1 and R3 in the S4 segment of a voltage sensor appears to facilitate the early stage of the motion toward a down state. We use multiple microsecond-steered molecular simulations to calculate the work required for translating S4 both as α-helix and transformed to 3(10)-helix. The barrier appears to be caused by salt-bridge reformation simultaneous to R4 passing the F233 hydrophobic lock, and it is almost a factor-two lower with 3(10)-helix. The latter facilitates translation because R2/R3 line up to face E183/E226, which reduces the requirement to rotate S4. This is also reflected in a lower root mean-square deviation distortion of the rest of the voltage sensor. This supports the 3(10) hypothesis, and could explain some of the differences between the open-inactivated- versus activated-states.
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