Structural Analysis of Botulinum Neurotoxin Type G Receptor Binding,
Copyright policy )Structural Analysis of Botulinum Neurotoxin Type G Receptor Binding,
Botulinum neurotoxin (BoNT) binds peripheral neurons at the neuromuscular junction through a dual-receptor mechanism that includes interactions with ganglioside and protein receptors. The receptor identities vary depending on BoNT serotype (A-G). BoNT/B and BoNT/G bind the luminal domains of synaptotagmin I and II, homologous synaptic vesicle proteins. We observe conditions under which BoNT/B binds both Syt isoforms, but BoNT/G binds only SytI. Both serotypes bind ganglioside G(T1b). The BoNT/G receptor-binding domain crystal structure provides a context for examining these binding interactions and a platform for understanding the physiological relevance of different Syt receptor isoforms in vivo.
- Medical College of Wisconsin United States
- Vanderbilt University United States
Models, Molecular, Botulinum Toxins, Protein Conformation, Gangliosides, Genetic Vectors, Receptors, Cell Surface, Crystallography, X-Ray, Protein Binding
Models, Molecular, Botulinum Toxins, Protein Conformation, Gangliosides, Genetic Vectors, Receptors, Cell Surface, Crystallography, X-Ray, Protein Binding
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