ArticleBiophysical journal2012
Molecular dynamics investigation of the ω-current in the Kv1.2 voltage sensor domains.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Computational Models of Claudin Assembly in Tight Junctions and Strand Properties.International journal of molecular sciences · 2024Review
- Anionic omega currents from single countercharge mutants in the voltage-sensing domain of Ci-VSP.The Journal of general physiology · 2024Article
- Computational Assessment of Different Structural Models for Claudin-5 Complexes in Blood-Brain Barrier Tight Junctions.ACS chemical neuroscience · 2022Article
- Kv3.1 channelopathy: a novel loss-of-function variant and the mechanistic basis of its clinical phenotypes.Annals of translational medicine · 2021Article
- Structural Mechanism of ω-Currents in a Mutated Kv7.2 Voltage Sensor Domain from Molecular Dynamics Simulations.Journal of chemical information and modeling · 2021Article
- Simulation of Gating Currents of the Shaker K Channel Using a Brownian Model of the Voltage Sensor.Biophysical journal · 2019Article
- Gating of Connexin Channels by transjunctional-voltage: Conformations and models of open and closed states.Biochimica et biophysica acta. Biomembranes · 2018Review
- A New Cardiac Channelopathy: From Clinical Phenotypes to Molecular Mechanisms Associated With NaFrontiers in cardiovascular medicine · 2018Review
- Atomistic Modeling of Ion Conduction through the Voltage-Sensing Domain of the Shaker KThe journal of physical chemistry. B · 2017Article
- Gating pore currents are defects in common with two Nav1.5 mutations in patients with mixed arrhythmias and dilated cardiomyopathy.The Journal of general physiology · 2015Article
- Domain and interdomain energetics underlying gating in Shaker-type Kv channels.Biophysical journal · 2014Article
- An effective coarse-grained model for biological simulations: recent refinements and validations.Proteins · 2014Article
- NaV1.4 mutations cause hypokalaemic periodic paralysis by disrupting IIIS4 movement during recovery.Brain : a journal of neurology · 2014Article
- Hydrophobic plug functions as a gate in voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Biophysics, pathophysiology, and pharmacology of ion channel gating pores.Frontiers in pharmacology · 2014Review
- Proton channel models filling the gap between experimental data and the structural rationale.Channels (Austin, Tex.) · 2014Review
- Integral membrane proteins and bilayer proteomics.Analytical chemistry · 2013Review
- Voltage-dependent gating of the Cx32*43E1 hemichannel: conformational changes at the channel entrances.The Journal of general physiology · 2013Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Mutations in KCND3 cause spinocerebellar ataxia type 22.Annals of neurology · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Voltage sensor domains (VSD) are transmembrane proteins that respond to changes in membrane voltage and modulate the activity of ion channels, enzymes, or in the case of proton channels allow permeation of protons across the cell membrane. VSDs consist of four transmembrane segments, S1-S4, forming an antiparallel helical bundle. The S4 segment contains several positively charged residues, mainly arginines, located at every third position along the helix. In the voltage-gated Shaker K(+) channel, the mutation of the first arginine of S4 to a smaller uncharged amino acid allows permeation of cations through the VSD. These currents, known as ω-currents, pass through the VSD and are distinct from K(+) currents passing through the main ion conduction pore. Here we report molecular dynamics simulations of the ω-current in the resting-state conformation for Kv1.2 and for four of its mutants. The four tested mutants exhibit various degrees of conductivity for K(+) and Cl(-) ions, with a slight selectivity for K(+) over Cl(-). Analysis of the ion permeation pathway, in the case of a highly conductive mutant, reveals a negatively charged constriction region near the center of the membrane that might act as a selectivity filter to prevent permeation of anions through the pore. The residues R1 in S4 and E1 in S2 are located at the narrowest region of the ω-pore for the resting state conformation of the VSD, in agreement with experiments showing that the largest increase in current is produced by the double mutation E1D and R1S.
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