High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6.

Clostridium botulinum X-ray crystallography binding domain structure botulinum neurotoxin subtypes

Journal

FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716

Informations de publication

Date de publication:
08 2020
Historique:
received: 18 06 2020
revised: 07 07 2020
accepted: 08 07 2020
pubmed: 13 7 2020
medline: 5 11 2021
entrez: 13 7 2020
Statut: ppublish

Résumé

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

Identifiants

pubmed: 32654405
doi: 10.1002/2211-5463.12931
pmc: PMC7396429
doi:

Substances chimiques

Botulinum Toxins, Type A EC 3.4.24.69

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1474-1481

Informations de copyright

© 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.

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Auteurs

Jonathan R Davies (JR)

Department of Biology and Biochemistry, Claverton Down, University of Bath, Bath, UK.
Department of Biochemistry and Biophysics, Stockholm University, Sweden.

Amy Britton (A)

Department of Biology and Biochemistry, Claverton Down, University of Bath, Bath, UK.

Sai Man Liu (SM)

Ipsen Bioinnovation Limited, Milton Park, Abingdon, UK.

K Ravi Acharya (KR)

Department of Biology and Biochemistry, Claverton Down, University of Bath, Bath, UK.

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