ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural basis for gating charge movement in the voltage sensor of a sodium channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.
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Who cites it
179 citing papers in PubMed.
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026Review
- Dose as a fundamental organizing principle in physiology: Implications for mechanism, disease, and precision medicine.Journal of precision medicine (Amsterdam, Netherlands) · 2026Article
- Nav1.8 Variant I206M as a Latent Susceptibility Factor in Postaxotomy Ocular Pain.Neurology. Genetics · 2026Article
- Infrared photons generated by voltage-gated sodium channel dynamics: a hypothesis for cooperative electrodynamic interactions at the axon initial segment.Frontiers in human neuroscience · 2026Review
- Article
- HInternational journal of molecular sciences · 2025Review
- The differential impacts of equivalent gating-charge mutations in voltage-gated sodium channels.The Journal of general physiology · 2025Article
- Understanding the role of mutations in voltage-gated sodium ion channels for cardiovascular disorders.The Journal of general physiology · 2025Article
- The evolution of patch-clamp electrophysiology: Robotic, multiplex, and dynamic.Molecular pharmacology · 2025Review
- Interior pH-sensing residue of human voltage-gated proton channel HBiophysical journal · 2024Article
- Structural biology of voltage-gated calcium channels.Channels (Austin, Tex.) · 2024Review
- A structural analysis of the splice-specific functional impact of the pathogenic familial hemiplegic migraine type 1 S218L mutation on CaMolecular brain · 2024Article
- Atomistic mechanisms of the regulation of small-conductance CaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- ELUCIDATING THE DIFFERENTIAL IMPACTS OF EQUIVALENT GATING-CHARGE MUTATIONS IN VOLTAGE-GATED SODIUM CHANNELS.bioRxiv : the preprint server for biology · 2024Article
- The chemistry of electrical signaling in sodium channels from bacteria and beyond.Cell chemical biology · 2024Review
- Bioelectricity in dental medicine: a narrative review.Biomedical engineering online · 2024Review
- Anionic omega currents from single countercharge mutants in the voltage-sensing domain of Ci-VSP.The Journal of general physiology · 2024Article
- Bioelectronic Medicine: a multidisciplinary roadmap from biophysics to precision therapies.Frontiers in integrative neuroscience · 2024Review
- Coevolution with toxic prey produces functional trade-offs in sodium channels of predatory snakes.bioRxiv : the preprint server for biology · 2023Article
- Article
119 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
Abstract
Voltage-dependent gating of ion channels is essential for electrical signaling in excitable cells, but the structural basis for voltage sensor function is unknown. We constructed high-resolution structural models of resting, intermediate, and activated states of the voltage-sensing domain of the bacterial sodium channel NaChBac using the Rosetta modeling method, crystal structures of related channels, and experimental data showing state-dependent interactions between the gating charge-carrying arginines in the S4 segment and negatively charged residues in neighboring transmembrane segments. The resulting structural models illustrate a network of ionic and hydrogen-bonding interactions that are made sequentially by the gating charges as they move out under the influence of the electric field. The S4 segment slides 6-8 Å outward through a narrow groove formed by the S1, S2, and S3 segments, rotates ∼30°, and tilts sideways at a pivot point formed by a highly conserved hydrophobic region near the middle of the voltage sensor. The S4 segment has a 3(10)-helical conformation in the narrow inner gating pore, which allows linear movement of the gating charges across the inner one-half of the membrane. Conformational changes of the intracellular one-half of S4 during activation are rigidly coupled to lateral movement of the S4-S5 linker, which could induce movement of the S5 and S6 segments and open the intracellular gate of the pore. We confirmed the validity of these structural models by comparing with a high-resolution structure of a NaChBac homolog and showing predicted molecular interactions of hydrophobic residues in the S4 segment in disulfide-locking studies.
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