Fig. 4: Predicted interface between BL3.2 and CTX.
From: Orally delivered toxin–binding protein protects against diarrhoea in a murine cholera model
a The most stable conformational binding arrangement between BL3.2 (green) and CTXB pentamer (grey) based on ColabFold and molecular dynamics simulations. b The nine amino acid residues in the complementarity-determining region one (CDR1) (Asp30 and Asp31), CDR2 (Asp55 and Ser57), and CDR3 (Tyr102, Asn104, Ser105, Gln107, and Asp111) of the BL3.2 paratope predicted to be essential for CTX binding. c The 14 amino acids in the CTXB epitope identified in silico to be crucial for BL3.2 interaction, nine in the primary CTXB (His13, Asn14, Ser55, Gln56, His57, Asp59, Gln61, Trp88, and Lys91) and five from the adjacent subunit in the pentamer (Lys34, Arg35, Glu36, Ser55, and Gln56).
