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Figure 4.
Figure 4 Comparison of Bcl-3 and I  B
 molecular
surfaces. The structures of I B
(A,
B, E and F) and Bcl-3 (C, D, G and H) are shown in equivalent
orientations. The view of (A) -(D) is orthogonal to that of (E)
-(H), which is approximately that of Figure 1B (i.e. with  -hairpins
on the left and 2
helices on the right.) (A, D, E and H) Comparison of
electrostatic surface potentials. Regions of negative and
positive potential are shown in red and blue, respectively. The
basic patch at the bottom of Bcl-3 is formed by arginine
residues 311, 318, 322, 342, 344, 345 and 351. The corresponding
surface of I B
is
formed by the acidic PEST region. (B, C, F and G) Conservation
of the NF- B
contact surface. The C-terminal domains of p50 (blue) and p65
(green) are represented as ribbons bound to the surface of I
B
and,
to facilitate comparison, to that of Bcl-3. In (B) and (F),
regions of the I B
surface
within 4.5 Å of the p50 and p65 RHR-c domains are colored
magenta. In (C) and (G), surface-exposed residues, which are
identically conserved between Bcl-3 and I B
,
are shown in yellow. The asterisks and triangles indicate
regions of the I B
surface
in contact with NF- B
that are composed of residues poorly conserved in Bcl-3. This
figure was prepared using GRASP (Nicholls et al., 1991).
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