ArticleScientific reports2015
Conotoxin αD-GeXXA utilizes a novel strategy to antagonize nicotinic acetylcholine receptors.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Deep learning-driven discovery and mechanism of action study of a minimalist conopeptide targetingActa pharmaceutica Sinica. B · 2026Article
- Diversity and Novelty of Venom Peptides in Vermivorous Cone Snails, SubgenusMarine drugs · 2025Article
- Unravelling the allosteric binding mode of αD-VxXXB at nicotinic acetylcholine receptors.Frontiers in pharmacology · 2023Article
- Synthesis of full-length homodimer αD-VxXXB that targets human α7 nicotinic acetylcholine receptors.RSC medicinal chemistry · 2022Article
- Article
- Marine Origin Ligands of Nicotinic Receptors: Low Molecular Compounds, Peptides and Proteins for Fundamental Research and Practical Applications.Biomolecules · 2022Review
- Conotoxin Diversity in the Venom Gland Transcriptome of the Magician's Cone,Marine drugs · 2019Article
- Article
- The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework.The Journal of biological chemistry · 2019Article
- High-Throughput Identification and Analysis of Novel Conotoxins from Three Vermivorous Cone Snails by Transcriptome Sequencing.Marine drugs · 2019Article
- Alanine-Scanning Mutagenesis of α-Conotoxin GI Reveals the Residues Crucial for Activity at the Muscle Acetylcholine Receptor.Marine drugs · 2018Article
- Discovery Methodology of Novel Conotoxins fromMarine drugs · 2018Review
- Neuronal Nicotinic Acetylcholine Receptor Modulators from Cone Snails.Marine drugs · 2018Review
- αO-Conotoxin GeXIVA disulfide bond isomers exhibit differential sensitivity for various nicotinic acetylcholine receptors but retain potency and selectivity for the human α9α10 subtype.Neuropharmacology · 2017Article
- Backbone cyclization of analgesic conotoxin GeXIVA facilitates direct folding of the ribbon isomer.The Journal of biological chemistry · 2017Article
- Identification of a Novel O-Conotoxin Reveals an Unusual and Potent Inhibitor of the Human α9α10 Nicotinic Acetylcholine Receptor.Marine drugs · 2017Article
- A Novel Lid-Covering Peptide Inhibitor of Nicotinic Acetylcholine Receptors Derived from αD-Conotoxin GeXXA.Marine drugs · 2017Article
- Inhibition of α9α10 nicotinic acetylcholine receptors prevents chemotherapy-induced neuropathic pain.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nicotinic acetylcholine receptors (nAChRs) play essential roles in transmitting acetylcholine-mediated neural signals across synapses and neuromuscular junctions, and are also closely linked to various diseases and clinical conditions. Therefore, novel nAChR-specific compounds have great potential for both neuroscience research and clinical applications. Conotoxins, the peptide neurotoxins produced by cone snails, are a rich reservoir of novel ligands that target receptors, ion channels and transporters in the nervous system. From the venom of Conus generalis, we identified a novel dimeric nAChR-inhibiting αD-conotoxin GeXXA. By solving the crystal structure and performing structure-guided dissection of this toxin, we demonstrated that the monomeric C-terminal domain of αD-GeXXA, GeXXA-CTD, retains inhibitory activity against the α9α10 nAChR subtype. Furthermore, we identified that His7 of the rat α10 nAChR subunit determines the species preference of αD-GeXXA, and is probably part of the binding site of this toxin. These results together suggest that αD-GeXXA cooperatively binds to two inter-subunit interfaces on the top surface of nAChR, thus allosterically disturbing the opening of the receptor. The novel antagonistic mechanism of αD-GeXXA via a new binding site on nAChRs provides a valuable basis for the rational design of new nAChR-targeting compounds.
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