Figure 3.
Fig. 3. The dimer interface and ligand-binding residues.
(A) Interacting residues in domain 1. Side chains are shown for
residues that interact across the dimer interface in domain 1
(Fig. 2A). The conserved central Val-51 residue is blue, and
Glu-34 is red. Salt bridges between residues at the periphery of
the interface are dashed lines. (B) Stereoview (40) of the
dimer. Side chains and carbons
are shown for residues important in binding to LFA-1 (red and
orange) (3, 37), human rhinoviruses 3, 14, 15, 36, and 41
(yellow and orange) (3-5), and P. falciparum (blue) (6). Only
single amino acid substitutions that reduced binding 50% or 2 SD
below control are shown.
carbons
are shown for residues important in binding to LFA-1 (red and
orange) (3, 37), human rhinoviruses 3, 14, 15, 36, and 41
(yellow and orange) (3-5), and P. falciparum (blue) (6). Only
single amino acid substitutions that reduced binding 50% or 2 SD
below control are shown.