Figure 1.

Sequence comparison and disulfide bridge arrangement of different neurotoxin structures from Cupiennius salei. Proposed C-terminal α-helical structures are shaded in light green and amino acid residues involved in forming the main part of loop 3 of the ICK structure are shaded in yellow/light brown. The possible docking region of heterodimeric neurotoxins and the proposed corresponding docking region of monomeric neurotoxins are boxed according to their charge. The involved cationic amino acid residues are in red and anionic amino acid residues are colored in blue. CT1-long and CT13-long are indicated by a box. Cysteines are highlighted in gray.