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Figure 3.
Figure 3 Interactions in the  -catenin
-APC-rA complex. (A) Comparison of -catenin-bound
APC-rA, XTcf3 and E-cadherin in the core homology region of
APC-rA. -catenin
residues are labeled in gray boxes. Other colors are as in
Figure 2B. Contacts between APC-rA and -catenin
are drawn as solid lines (non-polar interactions), dotted lines
(hydrogen bonds) or dashed lines (salt bridges). APC-rA residue
numbers are indicated in green. (B) Comparison of -catenin
bound APC-rA, XTcf3 and E-cadherin in the region of the APC-rA
bulge. Coloring and labeling is as in (A). Contacts of -catenin
with APC-rA are drawn in gray, and those with XTcf3 and
E-cadherin in red. (C) Stabilizing forces in the APC-rA
C-terminal bulge. -catenin
is drawn in a surface representation, colored blue for positive
and red for negative electrostatic potential at the 10 kT/e
level. The APC-rA peptide is colored by atom type with carbon
white, oxygen red and nitrogen blue. Although no density is seen
for the APC-rA Lys1030 or Asp1033 side chains in the structure,
they are modeled (gray side chains) to demonstrate their likely
interactions with regions of electrostatic potential on the
surface of -catenin.
Hydrogen bonds between backbone and side chain atoms within the
peptide are drawn as dotted lines. The Leu 1029 side chain is
not shown for clarity. (A) and (B) were generated using
Molscript and Raster3D (Kraulis, 1991; Merrit and Murphy, 1994).
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