Figure 3. Interactions between gp42 and HLA-DR1(A) Ribbon
diagram of the gp42:DR1 complex. gp42 is shown in red, DR1:HA in
blue. The N-terminal region of gp42 forms a two-stranded,
antiparallel β sheet with a crystallographically related
symmetry mate.(B) Interactions formed by DR1 Eβ46 with gp42
residues. The gp42 chain is shown in red and DR1 in blue. Eβ46
forms a salt bridge (R220) and a hydrogen bond (Y107) across the
interface, and single point mutations of Eβ46 have been shown
to affect EBV entry and gp42 binding.(C) Interactions formed by
DR1 Rβ72 with gp42 residues. Chains are colored as in (B).
Rβ72 interacts primarily with the backbone atoms of the turn
before the first β strand of the gp42 CTLD, including residues
104–107 and with the side chain of Y107. gp42 residues T104
and Y107 interact with both Eβ46 and Rβ72.
The above figure is reprinted
by permission from Cell Press: