Abstract
The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (HN) and a receptor-binding domain (HC). Here we report the crystal structure of HC/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our HC/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of HC/A1. This may have implications for receptor-binding and future recombinant toxin production.
Original language | English |
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Article number | e4552 |
Journal | PeerJ |
Volume | 6 |
DOIs | |
Publication status | Published - 21 Mar 2018 |
Keywords
- Botulinum neurotoxin
- Crystal structure
- FA hybrid
- Receptor binding domain
- SV2
- Targeted secretion inhibitor
ASJC Scopus subject areas
- General Neuroscience
- General Biochemistry,Genetics and Molecular Biology
- General Agricultural and Biological Sciences