Mutant cycle analysis with modified saxitoxins reveals specific interactions critical to attaining high-affinity inhibition of hNaV1.7.

doi:10.1073/pnas.1603486113

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Article

Mutant cycle analysis with modified saxitoxins reveals specific interactions critical to attaining high-affinity inhibition of hNaV1.7.

Proceedings of the National Academy of Sciences of the United States of America - 24 May 2016

Thomas-Tran Rhiannon, Du Bois J

Abstract excerpt

Improper function of voltage-gated sodium channels (NaVs), obligatory membrane proteins for bioelectrical signaling, has been linked to a number of human pathologies. Small-molecule agents that target NaVs hold considerable promise for treatment of chronic disease. Absent a comprehensive understanding of channel structure, the challenge of designing selective agents to modulate the activity of NaV subtypes is...

Topics

Animals
Binding Sites
CHO Cells
Cricetulus
Drug Design
Gene Expression
HEK293 Cells
Humans
Kinetics
Molecular Docking Simulation
Muscle Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

NAV1.2 Voltage-Gated Sodium Channel

NAV1.5 Voltage-Gated Sodium Channel

NAV1.7 Voltage-Gated Sodium Channel

Patch-Clamp Techniques

Protein Binding

Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 27162340
DOI: 10.1073/pnas.1603486113
PMCID: PMC4889396

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-27162340-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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