Residues and areas of individual monomers of tetrameric M2 ion channel interacted with the HuScFv. (A) Predicted M2 residues (black shades) in individual monomers of the ion channel which were bound by the HuScFv. (B) Results of molecular docking between the HuScFv with the tetrameric M2 ion channel template which was obtained from PDB entry 2LY0. (I) Interaction of HuScFv-2 (green), -19 (cyan), -23 (violet) and -27 (blue) with tetrameric M2 ion channel template. The so-obtained template contained only six residues of ectodomain (green), complete transmembrane helix (yellow) and 3 residues of amphipathic helix (pink) but lacked completely the C-terminal residues. (II) Regions (red shades) of individual M2 monomers (colored in light blue, light pink, light brown and pale yellow for monomers 1–4, respectively) that interacted with the HuScFv.