ArticleThe Journal of biological chemistry2015
Structural Insight into Specificity of Interactions between Nonconventional Three-finger Weak Toxin from Naja kaouthia (WTX) and Muscarinic Acetylcholine Receptors.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Blockers of Acetylcholine Receptors Affect the Hypotensive Effect of the Central Loop Fragment of the WTX Toxin.Doklady. Biochemistry and biophysics · 2026Article
- Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions.International journal of molecular sciences · 2025Review
- Variations in "Functional Site" Residues and Classification of Three-Finger Neurotoxins in Snake Venoms.Toxins · 2025Review
- Synthetic Peptide Fragments of the Wtx Toxin Reduce Blood Pressure in Rats under General Anesthesia.Doklady. Biochemistry and biophysics · 2023Article
- Comparison of Conformations and Interactions with Nicotinic Acetylcholine Receptors forInternational journal of molecular sciences · 2023Article
- Fifty Years of Animal Toxin Research at the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS.International journal of molecular sciences · 2023Review
- Membrane-mediated interaction of non-conventional snake three-finger toxins with nicotinic acetylcholine receptors.Communications biology · 2022Article
- Snake Venomics and Antivenomics of Cape Cobra (Toxins · 2022Article
- Structural and Functional Diversity of Animal Toxins Interacting With GPCRs.Frontiers in molecular biosciences · 2022Review
- Potassium channel blocker crafted by α-hairpinin scaffold engineering.Biophysical journal · 2021Article
- Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors.Molecules (Basel, Switzerland) · 2021Review
- Three-Finger Toxins from Brazilian Coral Snakes: From Molecular Framework to Insights in Biological Function.Toxins · 2021Article
- Human Three-Finger Protein Lypd6 Is a Negative Modulator of the Cholinergic System in the Brain.Frontiers in cell and developmental biology · 2021Article
- Structural Diversity and Dynamics of Human Three-Finger Proteins Acting on Nicotinic Acetylcholine Receptors.International journal of molecular sciences · 2020Article
- Novel Bradykinin-Potentiating Peptides and Three-Finger Toxins from Viper Venom: Combined NGS Venom Gland Transcriptomics and Quantitative Venom Proteomics of theBiomedicines · 2020Article
- Effects of Mlx-8, a phospholipase AThe journal of venomous animals and toxins including tropical diseases · 2020Article
- Protein surface topography as a tool to enhance the selective activity of a potassium channel blocker.The Journal of biological chemistry · 2019Article
- Cell-Free Expression of Sodium Channel Domains for Pharmacology Studies. Noncanonical Spider Toxin Binding Site in the Second Voltage-Sensing Domain of Human NaFrontiers in pharmacology · 2019Article
- Snake Venom Peptides: Tools of Biodiscovery.Toxins · 2018Review
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Weak toxin from Naja kaouthia (WTX) belongs to the group of nonconventional "three-finger" snake neurotoxins. It irreversibly inhibits nicotinic acetylcholine receptors and allosterically interacts with muscarinic acetylcholine receptors (mAChRs). Using site-directed mutagenesis, NMR spectroscopy, and computer modeling, we investigated the recombinant mutant WTX analogue (rWTX) which, compared with the native toxin, has an additional N-terminal methionine residue. In comparison with the wild-type toxin, rWTX demonstrated an altered pharmacological profile, decreased binding of orthosteric antagonist N-methylscopolamine to human M1- and M2-mAChRs, and increased antagonist binding to M3-mAChR. Positively charged arginine residues located in the flexible loop II were found to be crucial for rWTX interactions with all types of mAChR. Computer modeling suggested that the rWTX loop II protrudes to the M1-mAChR allosteric ligand-binding site blocking the entrance to the orthosteric site. In contrast, toxin interacts with M3-mAChR by loop II without penetration into the allosteric site. Data obtained provide new structural insight into the target-specific allosteric regulation of mAChRs by "three-finger" snake neurotoxins.
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