High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA

PeerJ

article

Jonathan R. Davies¹  Gavin S. Hackett²  Sai Man Liu²  K. Ravi Acharya¹ 

[1] Department of Biology and Biochemistry, University of Bath;Ipsen Bioinnovation Limited

关键词: SV2;    Crystal structure;    Botulinum neurotoxin;    Targeted secretion inhibitor;    FA hybrid;    Receptor binding domain;   

DOI  :  10.7717/peerj.4552

学科分类：社会科学、人文和艺术（综合）

来源: Inra

【 摘 要 】

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.

【 授权许可】

CC BY