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High‐resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6
Clostridium botulinum neurotoxins (BoNTs) cause flaccid paralysis through inhibition of acetylcholine release from motor neurons; however, at tiny doses, this property is exploited for use as a therapeutic. Each member of the BoNT family of proteins consists of three distinct domains: a binding doma...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7396429/ https://www.ncbi.nlm.nih.gov/pubmed/32654405 http://dx.doi.org/10.1002/2211-5463.12931 |
Sumario: | Clostridium botulinum neurotoxins (BoNTs) cause flaccid paralysis through inhibition of acetylcholine release from motor neurons; however, at tiny doses, this property is exploited for use as a therapeutic. Each member of the BoNT family of proteins consists of three distinct domains: a binding domain that targets neuronal cell membranes (H(C)), a translocation domain (H(N)) and a catalytic domain (LC). Here, we present high‐resolution crystal structures of the binding domains of BoNT subtypes/A5 (H(C)/A5) and/A6 (H(C)/A6). These structures show that the core fold identified in other subtypes is maintained, but with subtle differences at the expected receptor‐binding sites. |
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