ArticleThe Biochemical journal2013
Complex between α-bungarotoxin and an α7 nicotinic receptor ligand-binding domain chimaera.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 75 citations in OpenAlex.
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- Chimeric Approach to Identify Molecular Determinants of Nicotinic Acetylcholine Receptors.International journal of molecular sciences · 2026Review
- Cluster FLISA-A Method to Compare Protein Expression Efficiency Between Cell Lines and Subunit Clustering of Proteins.Bio-protocol · 2025Article
- Pro-angiogenic potential of the isoxazole derivative ISO-1 via α7-nAChRs activation in human endothelial cells.Biomedical reports · 2025Article
- HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors.Npj viruses · 2025Article
- N-Glycosylation Deficiency in Transgene α7 nAChR and RIC3 Expressing CHO Cells Without NACHO.The Journal of membrane biology · 2024Article
- A genetically engineered neuronal membrane-based nanotoxoid elicits protective immunity against neurotoxins.Bioactive materials · 2024Article
- Efficient Expression inMolecules (Basel, Switzerland) · 2024Article
- The human alpha7 nicotinic acetylcholine receptor is a host target for the rabies virus glycoprotein.Frontiers in cellular and infection microbiology · 2024Article
- 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
- The molecular mechanism of snake short-chain α-neurotoxin binding to muscle-type nicotinic acetylcholine receptors.Nature communications · 2022Article
- Protein Receptors Evolved from Homologous Cohesion Modules That Self-Associated and Are Encoded by Interactive Networked Genes.Life (Basel, Switzerland) · 2021Article
- Unbalanced Regulation of α7 nAChRs by Ly6h and NACHO Contributes to Neurotoxicity in Alzheimer's Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Pursuing High-Resolution Structures of Nicotinic Acetylcholine Receptors: Lessons Learned from Five Decades.Molecules (Basel, Switzerland) · 2021Review
- Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors.Molecules (Basel, Switzerland) · 2021Review
- Article
- Novel Three-Finger Neurotoxins fromToxins · 2021Article
- Human Three-Finger Protein Lypd6 Is a Negative Modulator of the Cholinergic System in the Brain.Frontiers in cell and developmental biology · 2021Article
- Nicotinic cholinergic system and COVID-19:Toxicology reports · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
To identify high-affinity interactions between long-chain α-neurotoxins and nicotinic receptors, we determined the crystal structure of the complex between α-btx (α-bungarotoxin) and a pentameric ligand-binding domain constructed from the human α7 AChR (acetylcholine receptor) and AChBP (acetylcholine-binding protein). The complex buries ~2000 Ų (1 Å=0.1 nm) of surface area, within which Arg³⁶ and Phe³² from finger II of α-btx form a π-cation stack that aligns edge-to-face with the conserved Tyr¹⁸⁴ from loop-C of α7, while Asp³⁰ of α-btx forms a hydrogen bond with the hydroxy group of Tyr¹⁸⁴. These inter-residue interactions diverge from those in a 4.2 Å structure of α-ctx (α-cobratoxin) bound to AChBP, but are similar to those in a 1.94 Å structure of α-btx bound to the monomeric α1 extracellular domain, although compared with the monomer-bound complex, the α-btx backbone exhibits a large shift relative to the protein surface. Mutational analyses show that replacing Tyr¹⁸⁴ with a threonine residue abolishes high-affinity α-btx binding, whereas replacing with a phenylalanine residue maintains high affinity. Comparison of the α-btx complex with that coupled to the agonist epibatidine reveals structural rearrangements within the binding pocket and throughout each subunit. The overall findings highlight structural principles by which α-neurotoxins interact with nicotinic receptors.
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