FIG 7.

Molecular docking of epitope II peptide to CD81-LEL. (A) Cartoon representation of one of three predominant conformations of epitope II peptide docked to CD81-LEL, with the C-α of residues W⁴³⁷LAGLF⁴⁴² restrained as a helix. Residues of the epitope II peptide and CD81-LEL are shown in stick representation. Backbone and side chain atoms of epitope II are indicated, with carbons shown in purple, oxygens in red, and nitrogens in blue. Atoms of backbone and side chain residues of CD81-LEL are also shown, with carbons in green, oxygens in red, and nitrogens in blue. (B) Cartoon representation of a predominant epitope II conformer obtained from docking to CD81-LEL with the C-α of residues W⁴³⁷LAGL⁴⁴¹ restrained as a helix, with less restriction than that in the conformer obtained for panel A. Residues in the epitope II peptide are shown in stick representation, with carbon atoms shown in metallic blue, oxygens in red, and nitrogens in blue. The color scheme for CD81-LEL atoms is the same as that for panel A. (C) Third representative conformer of epitope II docked to CD81-LEL, shown in cartoon representation. Docking was performed with W⁴³⁷LAGLF⁴⁴² restrained as a helix. The same color schemes as those denoted for panels A and B were used for all atoms but the carbons of epitope II, which are shown in metallic blue.