Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1
Figure 7
Functional pocket on the surface of gD.
Comparison between unliganded gD and gD/Nectin-1 complex. gD N-terminal residues 23–38 are green, the Ig-like V-domain is colored yellow (aa 56–185), the C-terminal region (aa 268–306) is shown in red and the remaining residues are white. A. In unliganded gD, the C-terminus of the ectodomain (red) is maintained in place by the insertion of Trp294 into a pocket made of the gD N-terminal residues, the α3-helix and residues from the Ig-core. This interaction is critical for function. B. The side chain of Phe129 (purple) located on the FG loop of the nectin-1 V-domain protrudes into the same pocket in the complex with gD. This binding configuration is not compatible with the native position of the gD C-terminus.