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Figure 2.
Figure 2. Structure of Unphosphorylated APC R3 Bound to
β-Catenin(A) Ribbon diagram of the complex, with cylinders
representing α helices. The β-catenin arm repeat domain is
shown in gray (helices 1 and 2 of the arm repeat motif) and cyan
(helix 3, which forms the groove) (Huber et al., 1997). The ICAT
helical domain used for crystallization is shown in white. The
superimposed crystal structures of the bound XTcf-3 (green),
E-cadherin (yellow), APC-RA (blue), and APC-R3 (orange) ligands
are shown.(B) Overlay of the extended peptide of R3 (orange) and
E-cadherin (yellow) bound to β-catenin. Nitrogen and oxygen
atoms are shown in blue and red, respectively. Residue numbers
for cadherin are shown in parentheses.(C) Diagram of the
interactions formed between APC R3 and β-catenin. APC residues
are shown in ovals with key side chain interactions indicated.
Hydrogen bonds and salt bridges are indicated by dashed lines,
and nonpolar contacts by arcs.
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