ArticleBiophysical journal2010
Down-state model of the voltage-sensing domain of a potassium channel.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Association of the P441L KCNQ1 variant with severity of long QT syndrome and risk of cardiac events.Frontiers in cardiovascular medicine · 2022Article
- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Voltage-Dependent Profile Structures of a Kv-Channel via Time-Resolved Neutron Interferometry.Biophysical journal · 2019Article
- Article
- Molecular pathogenesis of long QT syndrome type 1.Journal of arrhythmia · 2016Review
- Voltage Sensing in Membranes: From Macroscopic Currents to Molecular Motions.The Journal of membrane biology · 2015Review
- Electric fingerprint of voltage sensor domains.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Direct evidence of conformational changes associated with voltage gating in a voltage sensor protein by time-resolved X-ray/neutron interferometry.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.Biophysical journal · 2013Article
- Structural interactions between lipids, water and S1-S4 voltage-sensing domains.Journal of molecular biology · 2012Article
- The sliding-helix voltage sensor: mesoscale views of a robust structure-function relationship.European biophysics journal : EBJ · 2012Article
- Initial steps in the opening of a Shaker potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Coupling between the voltage-sensing and pore domains in a voltage-gated potassium channel.Biochimica et biophysica acta · 2012Article
- Tracking a complete voltage-sensor cycle with metal-ion bridges.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular dynamics investigation of the ω-current in the Kv1.2 voltage sensor domains.Biophysical journal · 2012Article
- Molecular dynamics simulations of voltage-gated cation channels: insights on voltage-sensor domain function and modulation.Frontiers in pharmacology · 2012Article
- Voltage-dependent gating of HERG potassium channels.Frontiers in pharmacology · 2012Article
- Ionic channels as targets for drug design: a review on computational methods.Pharmaceutics · 2011Article
- Article
- An electrostatic potassium channel opener targeting the final voltage sensor transition.The Journal of general physiology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-sensing domains (VSDs) of voltage-gated potassium (Kv) channels undergo a series of conformational changes upon membrane depolarization, from a down state when the channel is at rest to an up state, all of which lead to the opening of the channel pore. The crystal structures reported to date reveal the pore in an open state and the VSDs in an up state. To gain insights into the structure of the down state, we used a set of experiment-based restraints to generate a model of the down state of the KvAP VSD using molecular-dynamics simulations of the VSD in a lipid bilayer in excess water. The equilibrated VSD configuration is consistent with the biotin-avidin accessibility and internal salt-bridge data used to generate it, and with additional biotin-avidin accessibility data. In the model, both the S3b and S4 segments are displaced approximately 10 A toward the intracellular side with respect to the up-state configuration, but they do not move as a rigid body. Arginine side chains that carry the majority of the gating charge also make large excursions between the up and down states. In both states, arginines interact with water and participate in salt bridges with acidic residues and lipid phosphate groups. An important feature that emerges from the down-state model is that the N-terminal half of the S4 segment adopts a 3(10)-helical conformation, which appears to be necessary to satisfy a complex salt-bridge network.
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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.