Figure 6

Homology modeling and molecular docking between EtMIC3-bc1 protein and three target peptides. Secondary and tertiary structure of EtMIC3-bc1 protein were constructed, and an obvious hydrophobic groove was observed in three-dimensional (3D) structure of EtMIC3-bc1 which is responsible for binding target peptides (showed by arrow) (A). Molecular docking between EtMIC3-bc1 protein and peptide A, D and W was analyzed, respectively. All twelve amino acids in peptide A completely insert into the hydrophobic groove of EtMIC3-bc1 protein, and twelve hydrogen-bonds were formed between amino acids in peptide A and in EtMI3-bc1 protein (a and d, B). For peptide D, partial amino acids insert into the hydrophobic groove of EtMIC3-bc1 protein, and nine hydrogen-bonds were observed (b and e, B). Only several amino acids in peptide W insert into the hydrophobic groove of EtMIC3-bc1 protein, and six hydrogen-bonds were formed (c and f, B).