Fig. 8: Predicted hydrogen bond interactions of VHH TPL1158_01_C09 with α-cobratoxin (N. kaouthia), α-neurotoxin (D. polylepis), LCC, and α-bungarotoxin (B. multicinctus).
A Hydrogen bond interactions in the binding interface of the complex crystal structure of TPL1158_01_C09 (light blue) with α-cobratoxin (purple) mapped onto the respective paratope (bottom) and the epitope (top). The left close-up shows the predicted hydrogen bond network obtained from molecular dynamics simulations. The right close-up shows the local electron density map around the paratope/epitope region. B Hydrogen bond network obtained from molecular dynamics simulations mapped onto the respective epitope (top) and the paratope (bottom). The interactions for the α-cobratoxin complex are coloured in orange, for the α-neurotoxin (D. polylepis) complex in green, for the LCC complex in blue, and for the α-bungarotoxin complex in pink. The colour gradient corresponds to the probability of the respective interactions. C Sequence alignment with epitope residues highlighted in the colours corresponding with the structures in (B). A detailed paratope–epitope mapping per residue can be found in Supplementary Table S5.
