Figure 2
Crystal structure of the complex between Fab 10E8 and the 10E8ep peptide determined at 2.4 Å resolution in the presence of DPC.
(a) Overall structure of the complex. The surface of the heavy and light chains of the Fab are shown in light and dark gray, respectively. The peptide 10E8ep is depicted as a green helix. The hypothetical location of the viral membrane is shown (see Fig. 4 for more details). (b) Sigma-A weighted electron density map (blue mesh) of the peptide 10E8ep bound to the Fab at a contouring level of σ = 1.0. The peptide is depicted as green sticks. Numerous peptide hydrophobic residues (labeled) remain exposed even after engagement with the Fab. (c) H-bond network between peptide and Fab. Bond distances are shown. The peptide and Fab are depicted in green and gray sticks, respectively. (d) Interaction surface between peptide and Fab. The majority of interacting residues are non-polar. (e) Comparison of the conformation of the MPER peptide (PDB entry code 4G6F) and the optimized peptide (this study) bound to 10E8. The Fab and peptide from the previously published structure are depicted in magenta and orange, respectively. The Fab and peptide from this study are shown in light gray and green, respectively. Side-chains of residues Phe100aHC and Trp100bHC of the Fab, and Ile686 and Met687 of the peptide are depicted to illustrate additional interactions.
