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Figure 4.
Figure 4. Contacts between NF-κB and IκBα(a) The
backbone of IκBα is shown as an orange strand against the van
der Waals contact surface of NF-κB. The surface is colored dark
blue where the center of an atom of IκBα is within 3.8 Å
of an atom of NF-κB, and graded from light blue to white for
distances up to 4.5 Å. This figure is related by a
180° rotation relative to the view in Figure 1B. The thin
strip of continuity between the p50 contact (left) and the p65
contact (right) is the conserved salt-bridge network shown in
Figure 5B.(b) The backbones of the dimerization domains of
NF-κB are shown as orange strands against the van der Waals
contact surface of IκBα. This view is in the same orientation
as Figure 1B. Note how the fingers of IκBα project forward
toward the edge of the p50 RHR-c.(c) Residues of IκBα where
side chains make contacts with NF-κB are shown in color on a
space-filling representation of the ankyrin repeat stack. The
orientation of the model is the same as in Figure 1B and Figure
4B. Residues contacting the p50 RHR-c are in red; those
contacting p65 RHR-c are in dark blue; those contacting the p65
NLS and the segment C-terminal to it are in light blue. These
residues are also indicated by colored boxes in Figure 3A. (a)
and (b) were made using the program GRASP ( [45]), and (c),
using the program RIBBONS ( [13]).
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