ArticleNature structural & molecular biology2014
Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- The S1 helix is a VIP in VSP.The Journal of general physiology · 2024Article
- Cholesterol modulates the structural dynamics of the paddle motif loop of KvAP voltage sensor.Current research in structural biology · 2024Article
- Vascular mechanotransduction.Physiological reviews · 2023Review
- Not so optimal: The evolution of mutual information in potassium voltage-gated channels.PloS one · 2023Article
- Comparing the structural dynamics of the human KCNE3 in reconstituted micelle and lipid bilayered vesicle environments.Biochimica et biophysica acta. Biomembranes · 2022Article
- Mechanism of voltage sensing in CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.Nature structural & molecular biology · 2022Article
- Engineering of a synthetic antibody fragment for structural and functional studies of K+ channels.The Journal of general physiology · 2022Article
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins.Biomolecules · 2020Review
- Characterization of the Human KCNQ1 Voltage Sensing Domain (VSD) in Lipodisq Nanoparticles for Electron Paramagnetic Resonance (EPR) Spectroscopic Studies of Membrane Proteins.The journal of physical chemistry. B · 2020Article
- Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.eLife · 2020Article
- Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor.Biophysical journal · 2020Article
- The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix.Frontiers in molecular biosciences · 2020Article
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Article
- The voltage-gated sodium channel pore exhibits conformational flexibility during slow inactivation.The Journal of general physiology · 2018Article
- Site-Directed Spin Labeling EPR for Studying Membrane Proteins.BioMed research international · 2018Review
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Authors and funding
4 authors.
Funding
Abstract
Voltage-gated ion channels respond to transmembrane electric fields through reorientations of the positively charged S4 helix within the voltage-sensing domain (VSD). Despite a wealth of structural and functional data, the details of this conformational change remain controversial. Recent electrophysiological evidence showed that equilibrium between the resting ('down') and activated ('up') conformations of the KvAP VSD from Aeropyrum pernix can be biased through reconstitution in lipids with or without phosphate groups. We investigated the structural transition between these functional states, using site-directed spin-labeling and EPR spectroscopic methods. Solvent accessibility and interhelical distance determinations suggest that KvAP gates through S4 movements involving an ∼3-Å upward tilt and simultaneous ∼2-Å axial shift. This motion leads to large accessibly changes in the intracellular water-filled crevice and supports a new model of gating that combines structural rearrangements and electric-field remodeling.
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