ArticleNature2011
The crystal structure of a voltage-gated sodium channel.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 751 papers.
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Who cites it
751 citing papers in PubMed.
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026Review
- Electrostatic tuning of NaThe Journal of physiology · 2026Article
- Potassium channels in cancer: from hallmarks to therapeutic targeting.Journal of physiology and biochemistry · 2026Review
- Non-canonical pore architecture underlies constitutive gating of human retinal TRPM1.Nature communications · 2026Article
- Voltage-Gated Sodium Channel NaBiochemical genetics · 2026Article
- When can AlphaFold predict the oligomeric states of proteins?Protein science : a publication of the Protein Society · 2026Article
- Integrated Screening Cascades for Ion-Channel Drug Discovery: Linking Structure, Electrophysiology, Safety Pharmacology, and Human-Relevant Models.International journal of molecular sciences · 2026Review
- Volatile anaesthetics modulate voltage-gated sodium channel function at a site directly linked to channel gating.Nature communications · 2026Article
- Voltage-gated sodium channels in the nervous system: Molecular physiology to therapeutic interventions.Neural regeneration research · 2026Article
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.Science advances · 2026Article
- Structure-function analysis of the lithium-ion selectivity of the voltage-gated sodium channel.The Journal of general physiology · 2026Article
- Biochemical assessment of α-α-subunit interactions of NaScientific reports · 2026Article
- Cytochrome P450 inhibition impedes the insecticide pyrethroid effects on insects through Nav channels regulation.BMC biology · 2026Article
- Cryo-EM structure of TRPM1 reveals a non-canonical architecture with an inverted transmembrane domain.Nature communications · 2026Article
- Targeting NaInternational journal of molecular sciences · 2026Review
- Suzetrigine, a NaMolecules (Basel, Switzerland) · 2026Review
- 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
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.bioRxiv : the preprint server for biology · 2025Article
- Ion Channel-Targeting Toxins: Structural Mechanisms of Activation, Inhibition, and Therapeutic Potential.Toxins · 2025Review
- Structural and mechanistic insights into symmetry conversion in plant GORK K+ channel regulation.Protein & cell · 2025Article
691 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Voltage-gated sodium (Na(V)) channels initiate electrical signalling in excitable cells and are the molecular targets for drugs and disease mutations, but the structural basis for their voltage-dependent activation, ion selectivity and drug block is unknown. Here we report the crystal structure of a voltage-gated Na(+) channel from Arcobacter butzleri (NavAb) captured in a closed-pore conformation with four activated voltage sensors at 2.7 Å resolution. The arginine gating charges make multiple hydrophilic interactions within the voltage sensor, including unanticipated hydrogen bonds to the protein backbone. Comparisons to previous open-pore potassium channel structures indicate that the voltage-sensor domains and the S4-S5 linkers dilate the central pore by pivoting together around a hinge at the base of the pore module. The NavAb selectivity filter is short, ∼4.6 Å wide, and water filled, with four acidic side chains surrounding the narrowest part of the ion conduction pathway. This unique structure presents a high-field-strength anionic coordination site, which confers Na(+) selectivity through partial dehydration via direct interaction with glutamate side chains. Fenestrations in the sides of the pore module are unexpectedly penetrated by fatty acyl chains that extend into the central cavity, and these portals are large enough for the entry of small, hydrophobic pore-blocking drugs. This structure provides the template for understanding electrical signalling in excitable cells and the actions of drugs used for pain, epilepsy and cardiac arrhythmia at the atomic level.
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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.