Fig. 3

Structure of Fab(A10)/EGFR-derived peptide. (a) Structure of Fab(A10)/peptide in ribbon representation. The heavy chain is in purple and the light chain in pink. The bound peptide is in a β-hairpin conformation and colored green. The disulfide bond formed between residues C302 and C287 is shown in yellow sticks and labeled. (b) Surface representation of Fab(A10). The structure of Fab(A10)/peptide is shown in the same orientation as in (a), with the antibody rendered as molecular surface, which is colored by electrostatic surface potential. A red surface is a negative potential, whereas a blue surface is a positive potential. White surfaces are neutral. The electrostatic potential surface of the bound peptide is represented in the same orientation as in (a) or rotated 90°, showing the charge complementarity of antibody binding surface with that of the peptide epitope. (c) Superposition of A10/peptide with 806/peptide. The light chain (LC) and heavy chain (HC) of A10 are colored purple and blue, respectively. The LC and HC of 806 are in light and dark gray. The peptide bound to A10 is colored green and that of 806 in black. d) Electrostatic potential surface of Fab(806) in the same orientation as in (c). The bound peptide is rendered as a cartoon given in two orthogonal orientations. The electrostatic potential surface of the bound peptide in the same orientation as in (c) and rotated 90° showing the charge complementarity of antibody binding surface with that of the peptide epitope.