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  • Title: High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6.
    Author: Davies JR, Britton A, Liu SM, Acharya KR.
    Journal: FEBS Open Bio; 2020 Aug; 10(8):1474-1481. PubMed ID: 32654405.
    Abstract:
    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 (HC ), a translocation domain (HN ) and a catalytic domain (LC). Here, we present high-resolution crystal structures of the binding domains of BoNT subtypes/A5 (HC /A5) and/A6 (HC /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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