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Article

Mechanism of μ-conotoxin PIIIA binding to the voltage-gated Na+ channel NaV1.4.

PloS one - 1 Jan 2014

Chen Rong, Robinson Anna, Chung Shin-Ho

Abstract excerpt

Several subtypes of voltage-gated Na+ (NaV) channels are important targets for pain management. μ-Conotoxins isolated from venoms of cone snails are potent and specific blockers of different NaV channel isoforms. The inhibitory effect of μ-conotoxins on NaV channels has been examined extensively, but the mechanism of toxin specificity has not been understood in detail. Here the known structure of μ-conotoxin...

Topics

Amino Acid Sequence
Binding Sites
Conotoxins
Humans
Ions
Models, Molecular
Molecular Docking Simulation
Molecular Dynamics Simulation
Molecular Sequence Data
Mutation
NAV1.4 Voltage-Gated Sodium Channel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Conformation

Sequence Alignment

Structure-Activity Relationship

Source

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Identifiers

PMID: 24676211
DOI: 10.1371/journal.pone.0093267
PMCID: PMC3968119

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-24676211-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mechanism of μ-conotoxin PIIIA binding to the voltage-gated Na+ channel NaV1.4.PMID 24676211Read ↗

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