Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1
Figure 1
Structure of the gD/Nectin-1 complex.
A. Schematic representations of human nectin-1 and HSV-1 gD. Signal peptides are shown as white boxes and transmembrane regions are shown as hatched boxes. Lollipops represent N-glycosylation sites. For nectin-1, numbering starts at methionine 1 of the open reading frame while for gD it starts at lysine 1 of the mature glycoprotein. Arrowheads indicate the location of truncations for production of nectin-1(346t), gD285t, gD306t and gD316t. Nectin-1 is colored in violet with a region previously implicated in gD binding colored in red. The gD Ig core is in shown in yellow, residues forming the HVEM binding hairpin are in green, residues 39 to 55 from the N-terminal extension are in dark grey, residues 185 to 250 from the C-terminal extension are in light gray and residues 251 to 316 are in red. B. Ribbon representation of the gD/Nectin-1 complex. The color code is the same as in Fig. 1A. The secondary structure elements are labeled as in Carfi et al. [21]. The β-strands are labeled according to the Ig V-fold. Unsolved loops in the distal portion of the nectin-1 C1 domain are drawn as dotted lines.