ArticleNature communications2022
The molecular mechanism of snake short-chain α-neurotoxin binding to muscle-type nicotinic acetylcholine receptors.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 56 citations in OpenAlex.
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Antigenic divergence of cobra short-chain α-neurotoxins: Implications for regional antivenom effectiveness in Southeast Asia.PLoS neglected tropical diseases · 2026Article
- BiToxNet: a deep learning framework integrating multimodal features for accurate identification of neurotoxic peptides and proteins.BMC biology · 2026Article
- Development of a novel alpha7-nicotinic acetylcholine receptor-selective cell-penetrating peptide for intracellular cargo transport.Drug delivery · 2025Article
- Protective effects of clinical anticholinergic and anticholinesterase agents against Bungarus multicinctus venom and neurotoxin-rich snake venoms.PLoS neglected tropical diseases · 2025Article
- The role of acetylcholine and its receptors in tumor immune regulation: mechanisms and potential therapeutic targets.Molecular cancer · 2025Review
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- Red-on-Yellow Queen: Bio-Layer Interferometry Reveals Functional Diversity Within Micrurus Venoms and Toxin Resistance in Prey Species.Journal of molecular evolution · 2024Article
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- Influence of lipid bilayer on the structure of the muscle-type nicotinic acetylcholine receptor.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Cloning and Characterization of a Three-Finger Toxin Homolog (NXH8) from the CoralsnakeToxins · 2024Article
- Targeting Alpha7 Nicotinic Acetylcholine Receptors in Lung Cancer: Insights, Challenges, and Therapeutic Strategies.ACS pharmacology & translational science · 2024Review
- Article
Corrections and comments
- Erratum issued
Authors and funding
11 authors at 6 institutions in 6 countries.
Funding
Abstract
Bites by elapid snakes (e.g. cobras) can result in life-threatening paralysis caused by venom neurotoxins blocking neuromuscular nicotinic acetylcholine receptors. Here, we determine the cryo-EM structure of the muscle-type Torpedo receptor in complex with ScNtx, a recombinant short-chain α-neurotoxin. ScNtx is pinched between loop C on the principal subunit and a unique hairpin in loop F on the complementary subunit, thereby blocking access to the neurotransmitter binding site. ScNtx adopts a binding mode that is tilted toward the complementary subunit, forming a wider network of interactions than those seen in the long-chain α-Bungarotoxin complex. Certain mutations in ScNtx at the toxin-receptor interface eliminate inhibition of neuronal α7 nAChRs, but not of human muscle-type receptors. These observations explain why ScNtx binds more tightly to muscle-type receptors than neuronal receptors. Together, these data offer a framework for understanding subtype-specific actions of short-chain α-neurotoxins and inspire strategies for design of new snake antivenoms.
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