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Publication Abstract from PubMed

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.

High resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6.,Davies JR, Britton A, Liu SM, Acharya KR FEBS Open Bio. 2020 Jul 11. doi: 10.1002/2211-5463.12931. PMID:32654405^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.