ArticleToxins2018
Crystal Structure of Botulinum Neurotoxin A2 in Complex with the Human Protein Receptor SV2C Reveals Plasticity in Receptor Binding.
Article in Toxins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed.
- Structures of native SV2A reveal the binding mode for tetanus neurotoxin and anti-epileptic racetams.Nature communications · 2025Article
- Cryo-EM structure of the botulinum neurotoxin A/SV2B complex and its implications for translocation.Nature communications · 2025Article
- Structures of synaptic vesicle protein 2A and 2B bound to anticonvulsants.Nature structural & molecular biology · 2024Article
- Activity of botulinum neurotoxin X and its structure when shielded by a non-toxic non-hemagglutinin protein.Communications chemistry · 2024Article
- Structural basis for antiepileptic drugs and botulinum neurotoxin recognition of SV2A.Nature communications · 2024Article
- Structural basis for botulinum neurotoxin E recognition of synaptic vesicle protein 2.Nature communications · 2023Article
- Split luciferase-based assay to detect botulinum neurotoxins using hiPSC-derived motor neurons.Communications biology · 2023Article
- A Comprehensive Structural Analysis ofToxins · 2023Review
- Structural Features ofToxins · 2022Article
- Synaptic Vesicle Glycoprotein 2A: Features and Functions.Frontiers in neuroscience · 2022Review
- Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins.Microorganisms · 2021Review
- Knockin mouse models demonstrate differential contributions of synaptotagmin-1 and -2 as receptors for botulinum neurotoxins.PLoS pathogens · 2021Article
- Current Understanding of the Structure and Function of Pentapeptide Repeat Proteins.Biomolecules · 2021Review
- The Structure and Classification of Botulinum Toxins.Handbook of experimental pharmacology · 2021Article
- High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6.FEBS open bio · 2020Article
- Variations in the Botulinum Neurotoxin Binding Domain and the Potential for Novel Therapeutics.Toxins · 2018Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Botulinum neurotoxins (BoNTs) are a family of highly dangerous bacterial toxins, with seven major serotypes (BoNT/A-G). Members of BoNTs, BoNT/A1 and BoNT/B1, have been utilized to treat an increasing number of medical conditions. The clinical trials are ongoing for BoNT/A2, another subtype of BoNT/A, which showed promising therapeutic properties. Both BoNT/A1 and BoNT/A2 utilize three isoforms of synaptic vesicle protein SV2 (SV2A, B, and C) as their protein receptors. We here present a high resolution (2.0 Å) co-crystal structure of the BoNT/A2 receptor-binding domain in complex with the human SV2C luminal domain. The structure is similar to previously reported BoNT/A-SV2C complexes, but a shift of the receptor-binding segment in BoNT/A2 rotates SV2C in two dimensions giving insight into the dynamic behavior of the interaction. Small differences in key residues at the binding interface may influence the binding to different SV2 isoforms, which may contribute to the differences between BoNT/A1 and BoNT/A2 observed in the clinic.
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Registered trials
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