ArticleNature communications2024
Dual receptor-sites reveal the structural basis for hyperactivation of sodium channels by poison-dart toxin batrachotoxin.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Integrated Multi-Cohort Transcriptomic Analysis Reveals Molecular Networks and Signaling Pathway Landscape of Aconitine-Induced Cardiotoxicity and Myocardial Injury.Cardiovascular toxicology · 2026Article
- Batrachotoxin-sensitive sodium channels in toxic birds challenge "target mutation" strategy of toxin autoresistance.iScience · 2026Article
- Structural and functional mechanisms underlying activation gate dynamics and IFM motif accessibility in human NaNature communications · 2026Article
- Modulation of ion channels as emerging therapeutic targets in the treatment of diabetic neuropathy.EXCLI journal · 2026Review
- Bottom-up design of CaNature · 2025Article
- Article
- Structural basis of human NaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Drugs exhibit diverse binding modes and access routes in the Nav1.5 cardiac sodium channel pore.The Journal of general physiology · 2025Article
- Pioneering pain management with botulinum toxin type A: From anti-inflammation to regenerative therapies.Heliyon · 2025Review
- Harnessing Deep Learning Methods for Voltage-Gated Ion Channel Drug Discovery.Physiology (Bethesda, Md.) · 2025Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
The poison dart toxin batrachotoxin is exceptional for its high potency and toxicity, and for its multifaceted modification of the function of voltage-gated sodium channels. By using cryogenic electron microscopy, we identify two homologous, but nonidentical receptor sites that simultaneously bind two molecules of toxin, one at the interface between Domains I and IV, and the other at the interface between Domains III and IV of the cardiac sodium channel. Together, these two bound toxin molecules stabilize α/π helical conformation in the S6 segments that gate the pore, and one of the bound BTX-B molecules interacts with the crucial Lys1421 residue that is essential for sodium conductance and selectivity via an apparent water-bridged hydrogen bond. Overall, our structure provides insight into batrachotoxin's potency, efficacy, and multifaceted functional effects on voltage-gated sodium channels via a dual receptor site mechanism.
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