ArticleJournal of molecular biology2010
Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Leaflet-specific effects of charged lipids on a voltage-gated potassium channel.Journal of lipid research · 2025Article
- Cotranslational membrane insertion of the voltage-sensitive KProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lipid probes to study ion channels.Current opinion in chemical biology · 2025Review
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- N-Terminus-Mediated Solution Structure of Dimerization Domain of PRC1.Current issues in molecular biology · 2022Article
- Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.eLife · 2020Article
- The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix.Frontiers in molecular biosciences · 2020Article
- Cryo-EM structure of the KvAP channel reveals a non-domain-swapped voltage sensor topology.eLife · 2019Article
- CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.Journal of biomolecular NMR · 2019Article
- Competitive Interactions between PIRT, the Cold Sensing Ion Channel TRPM8, and PIPScientific reports · 2019Article
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Article
- Regulation of KCNQ/Kv7 family voltage-gated KBiochimica et biophysica acta. Biomembranes · 2017Review
- Disulfide mapping the voltage-sensing mechanism of a voltage-dependent potassium channel.Scientific reports · 2016Article
- Molecular basis of the interaction between gating modifier spider toxins and the voltage sensor of voltage-gated ion channels.Scientific reports · 2016Article
- Molecular dynamics simulation strategies for protein-micelle complexes.Biochimica et biophysica acta · 2016Article
- Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015Review
- An extended combinatorial 15N, 13Cα, and 13C' labeling approach to protein backbone resonance assignment.Journal of biomolecular NMR · 2015Article
- Voltage Sensing in Membranes: From Macroscopic Currents to Molecular Motions.The Journal of membrane biology · 2015Review
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2 authors.
Funding
Abstract
Voltage-sensor domains (VSDs) are specialized transmembrane segments that confer voltage sensitivity to many proteins such as ion channels and enzymes. The activities of these domains are highly dependent on both the chemical properties and the physical properties of the surrounding membrane environment. To learn about VSD-lipid interactions, we used nuclear magnetic resonance spectroscopy to determine the structure and phospholipid interface of the VSD from the voltage-dependent K(+) channel KvAP (prokaryotic Kv from Aeropyrum pernix). The solution structure of the KvAP VSD solubilized within phospholipid micelles is similar to a previously determined crystal structure solubilized by a nonionic detergent and complexed with an antibody fragment. The differences observed include a previously unidentified short amphipathic α-helix that precedes the first transmembrane helix and a subtle rigid-body repositioning of the S3-S4 voltage-sensor paddle. Using (15)N relaxation experiments, we show that much of the VSD, including the pronounced kink in S3 and the S3-S4 paddle, is relatively rigid on the picosecond-to-nanosecond timescale. In contrast, the kink in S3 is mobile on the microsecond-to-millisecond timescale and may act as a hinge in the movement of the paddle during channel gating. We characterized the VSD-phospholipid micelle interactions using nuclear Overhauser effect spectroscopy and showed that the micelle uniformly coats the KvAP VSD and approximates the chemical environment of a phospholipid bilayer. Using paramagnetically labeled phospholipids, we show that bilayer-forming lipids interact with the S3 and S4 helices more strongly than with S1 and S2.
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