Davies Jonathan R, Hackett Gavin S, Liu Sai Man, Acharya K Ravi
Department of Biology and Biochemistry, University of Bath, Bath, United Kingdom.
Ipsen Bioinnovation Limited, Abingdon, United Kingdom.
PeerJ. 2018 Mar 21;6:e4552. doi: 10.7717/peerj.4552. eCollection 2018.
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 (H) and a receptor-binding domain (H). Here we report the crystal structure of H/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our H/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of H/A1. This may have implications for receptor-binding and future recombinant toxin production.
肉毒杆菌神经毒素（BoNTs）的结合特异性主要是其能够同时结合多种受体的结果。BoNTs由三个不同的结构域组成，一个金属蛋白酶轻链（LC）、一个转位结构域（H）和一个受体结合结构域（H）。在此，我们报告了H/FA的晶体结构，通过对一个先前未解析的、对受体结合很重要的环进行建模，补充了现有结构。我们的H/FA结构还包含一个先前未鉴定的二硫键，我们在H/A1的两种晶体形式之一中也观察到了该二硫键。这可能对受体结合和未来重组毒素的生产有影响。
