Structural highlights
Publication Abstract from PubMed
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.
High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA.,Davies JR, Hackett GS, Liu SM, Acharya KR PeerJ. 2018 Mar 21;6:e4552. doi: 10.7717/peerj.4552. eCollection 2018. PMID:29576992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Davies JR, Hackett GS, Liu SM, Acharya KR. High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA. PeerJ. 2018 Mar 21;6:e4552. doi: 10.7717/peerj.4552. eCollection 2018. PMID:29576992 doi:http://dx.doi.org/10.7717/peerj.4552
