1. Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor HveA
Andrea Carfı́, Sharon H. Willis, J.Charles Whitbeck, Claude Krummenacher, Gary H. Cohen, Roselyn J. Eisenberg, Don C. Wiley 
Molecular Cell 
Volume 8, Issue 1, Pages (July 2001)
DOI: /S (01)

2. Figure 1 Structural Analysis of gD and gD-HveA Complex
(A) Ribbon diagram of gD285-HveA162 complex. gD is colored in red and HveA in green. Only the first 32 residues of gD (part of the hairpin 1–32) are involved in receptor binding. The core of gD (residues 56 to184) adopts a V-like Ig fold. The Ig-like β strands A′GFCC′C″ form the β sheet at the back and BED the β sheet in the front. Four additional β strands (β1 and β2 precede the Ig-like domain and β3 and β4 follow it) and three α helices are also labeled.
(B) Superposition of gD285 and the D1 domain of CD58. The gD Ig-core is in yellow. The N- and C-terminal extensions of gD (1 to 55 and 185 to 259, respectively) are in gray, and CD58 is in green.
(C) gD285 structure viewed 180° from (b). Colored as (b).
Figures 1, 2, 3A, 3C, 5B, 6A, and 6B were generated with MOLSCRIPT (Kraulis, 1991) and RASTER3D (Bacon and Andreson, 1988). Figures 3B and 6A were generated with GRASP (Nicholls et al., 1991)
Molecular Cell 2001 8, DOI: ( /S (01) )

3. Figure 2
Structural and Sequence Comparisons between HveA and Other TNFR Family Members
(A) HveA with TNFR-1 superimposed. TNFR-1 CRD1 (red) and CRD2 (blue) were superimposed separately (arrow at separation) on HveA (green).
(B) Structure based sequence alignment between TNFR-SF members. HveA has a 28% sequence identity with TNFR-1 over the first 100 residues, but the sequences diverge beyond that (Altschul et al., 1997). The sequences aligned are in the order: human-HveA, mouse-CD40, human-TNFR-1, human-TNFR-2. Each CRD can be subdivided in two structural entities or modules. For HveA and TNFR-1, each module has been named (a1, b2, etc.) according to the definition adopted by Naismith (Naismith and Sprang, 1998). Within each CRD, cysteines forming disulfide bonds (based on TNFR-1 structure) are in the same color. N-linked glycoslation sites in HveA are marked with lollipops
Molecular Cell 2001 8, DOI: ( /S (01) )

4. Figure 3 The gD-HveA Interface
(A) A schematic representation of the N-terminal hairpin of gD (red) and the three HveA (green) segments that contact gD.
(B) Contact surface on gD (red labels; blue patch on gray gD surface) and the three segments of HveA residues (green; 17 to 26, 30 to 39, and 74 to 76, and Cys 19 to Cys 37 disulfide bond) containing atoms which are closer than 4 Å to gD. Hydrogen bonds are shown as white dotted lines. This is viewed as in (A).
(C) Stereographic diagram of the contacts in the interface of gD (white) and HveA (yellow). Dashed red lines are probable hydrogen bonds
Molecular Cell 2001 8, DOI: ( /S (01) )

5. Figure 4
Amino Acid Sequence Alignments of the gD Ectodomains of Human and Animal α-Herpesviruses
The alignment was obtained with BLAST (Altschul et al., 1997). The sequences of HSV-1, HSV-2, Prv, and BHV-1 gDs are shown. Highlighted in yellow are residues that are strictly conserved both in HSVs and in either of the animal herpes viruses gDs
Molecular Cell 2001 8, DOI: ( /S (01) )

6. Figure 5 Conformational Change in the N Terminus of gD
(A) gD285, as in the structure of gD285-HveA complex, viewed end-on (left end of Figure 1A) and showing the N-terminal HveA binding hairpin (red) backed by the 224–240 α-helix (white).
(B) Structure of gD285 in the unliganded state. Viewed as in Figure 5A. Residues 1–14 are not visible in electron density maps and presumed disordered (see Methods)
Molecular Cell 2001 8, DOI: ( /S (01) )

7. Figure 6 Ion Binding Sites S1 and S2, Probably Sulfates, on gD
(A) Electrostatic potential surface of gD (same orientation as in Figure 1A). Positive potential (>14 mv; blue), neutral potential (0 mv; gray), and negative potential (<−14 mv; red) were calculated using GRASP (Nicholls et al., 1991). S1 binds in a positively charged pocket near the HveA (green) interface. S2 binds on a flat surface covered with basic residues.
(B) The S1 ion binding pocket. Arg130 forms salt-bridged hydrogen bonds with a presumptive sulfate ion (green and red). Other basic residues are listed in the text.
(C) The S2 ion binding surface. Colored as (B)
Molecular Cell 2001 8, DOI: ( /S (01) )