Figure 2.
Figure 2: Structure of the Cdc42/f–ACK complex. a,
Stereoview of the backbone (C trace)
of residues 2–179 of Cdc42 and residues 504–543 of f-ACK
from the 20 lowest energy structures (out of 58 that converged
from the 100 computed). In the final structures, no distance
restraint was violated by more than 0.5 å and no dihedral
angle restraint by more than 6.0°. The structures have good
covalent geometry and non-bonded contacts (Table 2). b,
Representation of the structure closest to the mean in the same
orientation as that in a. c, Space-filled representation of the
Cdc42/f–ACK complex, showing the hairpin in ACK and the
interactions with switch II. f-ACK wraps around Cdc42 forming an
extensive interface, burying a surface area of 4,200
å^2 between the two molecules. The structure is rotated
120°
about the z -axis compared to b. Figures 2 and 3 were generated
using Molscript^29 and Raster3D^30. Cdc42 is in blue and f-ACK
is yellow.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1999,
399,
384-388)
copyright 1999.
trace)
of residues 2–179 of Cdc42 and residues 504–543 of f-ACK
from the 20 lowest energy structures (out of 58 that converged
from the 100 computed). In the final structures, no distance
restraint was violated by more than 0.5 å and no dihedral
angle restraint by more than 6.0°. The structures have good
covalent geometry and non-bonded contacts (Table 2). b,
Representation of the structure closest to the mean in the same
orientation as that in a. c, Space-filled representation of the
Cdc42/f–ACK complex, showing the hairpin in ACK and the
interactions with switch II. f-ACK wraps around Cdc42 forming an
extensive interface, burying a surface area of 
4,200
å^2 between the two molecules. The structure is rotated