ArticleNature communications2013
The pore of voltage-gated potassium ion channels is strained when closed.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 69 citations in OpenAlex.
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- Closed state structure of the pore revealed by uncoupled Shaker KNature communications · 2025Article
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- Characterizing fenestration size in sodium channel subtypes and their accessibility to inhibitors.Biophysical journal · 2022Article
- Weak Cation Selectivity in HCN Channels Results From KFunction (Oxford, England) · 2022Article
- Structural and molecular insight into the pH-induced low-permeability of the voltage-gated potassium channel Kv1.2 through dewetting of the water cavity.PLoS computational biology · 2020Article
- Challenges and advances in atomistic simulations of potassium and sodium ion channel gating and permeation.The Journal of physiology · 2019Review
- The Role of Proton Transport in Gating Current in a Voltage Gated Ion Channel, as Shown by Quantum Calculations.Sensors (Basel, Switzerland) · 2018Article
- Computational Study of the Loss-of-Function Mutations in the Kv1.5 Channel Associated with Atrial Fibrillation.ACS omega · 2018Article
- Effects of protein-protein interactions and ligand binding on the ion permeation in KCNQ1 potassium channel.PloS one · 2018Article
- Computational membrane biophysics: From ion channel interactions with drugs to cellular function.Biochimica et biophysica acta. Proteins and proteomics · 2017Review
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- TRPV1: A Target for Rational Drug Design.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Grafting voltage and pharmacological sensitivity in potassium channels.Cell research · 2016Article
- Kainate receptor pore-forming and auxiliary subunits regulate channel block by a novel mechanism.The Journal of physiology · 2016Article
- Calcium ions open a selectivity filter gate during activation of the MthK potassium channel.Nature communications · 2015Article
- Mechanism-Based Mathematical Model for Gating of Ionotropic Glutamate Receptors.The journal of physical chemistry. B · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-gated potassium channels form potassium-selective pores in cell membranes. They open or close in response to changes in the transmembrane potential and are essential for generating action potentials, and thus for the functioning of heart and brain. While a mechanism for how these channels close has been proposed, it is not clear what drives their opening. Here we use free energy molecular dynamics simulations to show that work must be done on the pore to reduce the kink in the pore-lining (S6) α-helices, thereby forming the helix bundle crossing and closing the channel. Strain is built up as the pore closes, which subsequently drives opening. We also determine the effect of mutating the PVPV motif that causes the kink in the S6 helix. Finally, an approximate upper limit on how far the S4 helix is displaced as the pore closes is estimated.
Identifiers
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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.