ArticleBiophysical journal2007
Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 135 citations in OpenAlex.
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- Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP.Nature communications · 2024Article
- Domain- and state-specific shape of the electric field tunes voltage sensing in voltage-gated sodium channels.Biophysical journal · 2023Article
- Mechanism of voltage sensing in CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Spontaneous local membrane curvature induced by transmembrane proteins.Biophysical journal · 2022Article
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- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Decrypting the Heat Activation Mechanism of TRPV1 Channel by Molecular Dynamics Simulation.Biophysical journal · 2018Article
- Toward elucidating the heat activation mechanism of the TRPV1 channel gating by molecular dynamics simulation.Proteins · 2016Article
- The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel.PLoS computational biology · 2016Article
- Functional diversity of potassium channel voltage-sensing domains.Channels (Austin, Tex.) · 2016Review
- Voltage Sensing in Membranes: From Macroscopic Currents to Molecular Motions.The Journal of membrane biology · 2015Review
- Conformational dynamics of shaker-type Kv1.1 ion channel in open, closed, and two mutated states.The Journal of membrane biology · 2015Article
- Voltage-dependent gating and gating charge measurements in the Kv1.2 potassium channel.The Journal of general physiology · 2015Article
- 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
- Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines.Biochimica et biophysica acta · 2015Article
- Electric fingerprint of voltage sensor domains.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
All-atom molecular dynamics simulations are used to better understand the dynamic environment experienced by the Kv1.2 channel in a lipid membrane. The structure of the channel is stable during the trajectories. The pore domain keeps a well-defined conformation, whereas the voltage-sensing domains undergo important lateral fluctuations, consistent with their modular nature. A channel-like region at the center of the S1-S4 helical bundle fills rapidly with water, reminiscent of the concept of high-dielectric aqueous crevices. The first two arginines along S4 (R294 and R297) adopt an interfacial position where they interact favorably with water and the lipid headgroups. The following two arginines (R300 and R303) interact predominantly with water and E226 in S2. Despite the absence of a structurally permanent gating pore formed by protein residues and surrounding the S4 helix, as traditionally pictured, the charged residues are located in a favorable environment and are not extensively exposed to the membrane nonpolar region. Continuum electrostatic computations indicate that the transmembrane potential sensed by the charged residues in the voltage sensor varies abruptly over the outer half of the membrane in the arginine-rich region of S4; thus, the voltage gradient or membrane electric field is "focused". Interactions of basic residues with the lipid headgroups at the intracellular membrane-solution interface reduce the membrane thickness near the channel, resulting in an increased transmembrane field.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.