Crystal structure of the receptor binding domain of the botulinum C–D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions (original) (raw)

The study investigates the crystal structure of the receptor binding domain of botulinum neurotoxin C-D mosaic (BoNT/CD-HCR) to understand its interactions with membranes and identify specific roles of lysines K1118 and K1136 in binding affinity to synaptosomes. By comparing the structures of BoNT/CD-HCR and BoNT/D-HCR, significant differences were found which may clarify underlying biological functions. The results highlight how these lysine residues impact binding interactions and provide insights for future research into bioterrorism risks and therapeutic development.