Figure 2.
Figure 2 Space-filling structural models for (A) a homology
model of the wild-type adhesion domain of CD58 depicting
surface-exposed hydrophobic residues and (B) the NMR structure
of 1dCD58[6m] depicting mutation sites. The molecules are viewed
edge-on, with -strands
A and B directly in the front. Proline and glycine residues are
colored in yellow, other hydrophobic residues in green, mutation
sites in red, and putative glycan attachment positions in blue.
The graphs were prepared using GRASP (Nicholls et al., 1991).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
2941-2949)
copyright 1999.
-strands
A and B directly in the front. Proline and glycine residues are
colored in yellow, other hydrophobic residues in green, mutation
sites in red, and putative glycan attachment positions in blue.
The graphs were prepared using GRASP (Nicholls et al., 1991).