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6TWO

Binding domain of BoNT/A6

This is a non-PDB format compatible entry.
Summary for 6TWO
Entry DOI10.2210/pdb6two/pdb
DescriptorBont/A1, CHLORIDE ION (3 entities in total)
Functional Keywordsbinding domain, botulinum neurotoxin, toxin
Biological sourceClostridium botulinum
Total number of polymer chains1
Total formula weight50717.10
Authors
Davies, J.R.,Britton, A.,Acharya, K.R. (deposition date: 2020-01-13, release date: 2020-07-22, Last modification date: 2024-01-24)
Primary citationDavies, J.R.,Britton, A.,Liu, S.M.,Acharya, K.R.
High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6.
Febs Open Bio, 10:1474-1481, 2020
Cited by
PubMed 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 (H ), a translocation domain (H ) and a catalytic domain (LC). Here, we present high-resolution crystal structures of the binding domains of BoNT subtypes/A5 (H /A5) and/A6 (H /A6). These structures show that the core fold identified in other subtypes is maintained, but with subtle differences at the expected receptor-binding sites.
PubMed: 32654405
DOI: 10.1002/2211-5463.12931
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.35 Å)
Structure validation

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