ArticleProceedings of the National Academy of Sciences of the United States of America2002
Experimentally based model of a complex between a snake toxin and the alpha 7 nicotinic receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 120 citations in OpenAlex.
- Identification and validation of LY6H and GRM3 as candidate biomarkers for Glioma-related epilepsy.Scientific reports · 2025Article
- Synthetic development of a broadly neutralizing antibody against snake venom long-chain α-neurotoxins.Science translational medicine · 2024Article
- The human alpha7 nicotinic acetylcholine receptor is a host target for the rabies virus glycoprotein.Frontiers in cellular and infection microbiology · 2024Article
- Synthetic Peptide Fragments of the Wtx Toxin Reduce Blood Pressure in Rats under General Anesthesia.Doklady. Biochemistry and biophysics · 2023Article
- Neurotoxins Acting at Synaptic Sites: A Brief Review on Mechanisms and Clinical Applications.Toxins · 2022Review
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- Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors.Molecules (Basel, Switzerland) · 2021Review
- Structure-Function of Neuronal Nicotinic Acetylcholine Receptor Inhibitors Derived From Natural Toxins.Frontiers in neuroscience · 2020Review
- A Decoy-Receptor Approach Using Nicotinic Acetylcholine Receptor Mimics Reveals Their Potential as Novel Therapeutics Against Neurotoxic Snakebite.Frontiers in pharmacology · 2019Article
- Receptor variability-driven evolution of snake toxins.Zoological research · 2018Article
- Article
- Complex between α-bungarotoxin and an α7 nicotinic receptor ligand-binding domain chimaera.The Biochemical journal · 2013Article
- Inter-residue coupling contributes to high-affinity subtype-selective binding of α-bungarotoxin to nicotinic receptors.The Biochemical journal · 2013Article
- Crystallization of recombinant green mamba ρ-Da1a toxin during a lyophilization procedure and its structure determination.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Water-soluble LYNX1 residues important for interaction with muscle-type and/or neuronal nicotinic receptors.The Journal of biological chemistry · 2013Article
- Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.PloS one · 2012Article
- Structural model of ligand-G protein-coupled receptor (GPCR) complex based on experimental double mutant cycle data: MT7 snake toxin bound to dimeric hM1 muscarinic receptor.The Journal of biological chemistry · 2011Article
- Inhibition of the nicotinic acetylcholine receptors by cobra venom α-neurotoxins: is there a perspective in lung cancer treatment?PloS one · 2011Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To understand how snake neurotoxins interact with nicotinic acetylcholine receptors, we have elaborated an experimentally based model of the alpha-cobratoxin-alpha7 receptor complex. This model was achieved by using (i) a three-dimensional model of the alpha7 extracellular domain derived from the crystallographic structure of the homologous acetylcholine-binding protein, (ii) the previously solved x-ray structure of the toxin, and (iii) nine pairs of residues identified by cycle-mutant experiments to make contacts between the alpha-cobratoxin and alpha7 receptor. Because the receptor loop F occludes entrance of the toxin binding pocket, we submitted this loop to a dynamics simulation and selected a conformation that allowed the toxin to reach its binding site. The three-dimensional structure of the toxin-receptor complex model was validated a posteriori by an additional double-mutant experiment. The model shows that the toxin interacts perpendicularly to the receptor axis, in an equatorial position of the extracellular domain. The tip of the toxin central loop plugs into the receptor between two subunits, just below the functional receptor loop C, the C-terminal tail of the toxin making adjacent additional interactions at the receptor surface. The receptor establishes major contacts with the toxin by its loop C, which is assisted by principal (loops A and B) and complementary (loops D, F, and 1) functional regions. This model explains the antagonistic properties of the toxin toward the neuronal receptor and opens the way to the design of new antagonists.
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