6two | pdb_00006two

Binding domain of BoNT/A6

spinqualitylabelsall models 6two, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6two is a 1 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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