 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
journal menu
![[Figure 2]](mv5090fig2mag.jpg)
|
|
Figure 2
Sequence alignment. (a) Schematic representation of HSV-2 gD. The constructed regions (residues 1–275) of gD in this study are represented in orange. N-linked oligosaccharides are shown as green lollipops and a predicted transmembrane (TM) region is highlighted in cyan. (b) gD protein sequence alignment between herpesviruses. The gD sequence from Herpes simplex virus type 2 (NCBI accession No. AAW23130) is aligned with those of the gD proteins of Herpes simplex virus type 1 (AAA19631) and Chimpanzee alpha-1 herpesvirus (BAE47060). Residues in α-helices, β-strands and disordered loops are shown as red cylinders, blue arrows and dotted lines, respectively. The residues involved in the antibody interaction in the gD–E317 complex are marked with yellow boxes (nonpolar interactions) and black stars (hydrogen bonding). (c) E317 sequence alignment. The amino-acid sequence of the V and J regions of E317 was aligned with the closest homologous germline suggested by IMGT/V-QUEST and junction analysis (Lefranc et al., 2012  ). The positions of the CDRs according to the IMGT nomenclature are indicated, whereas somatic mutations are shaded. The residues involved in the antigen interaction in the gD–E317 complex are marked with black dots. |
![[Figure 2]](mv5090fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
