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Figure 2.
Figure 2. The ICAT Helical Domain(A) Structure of the
helical domain showing key hydrophobic core packing
interactions. Helices A, B, and C are indicated.(B) Hydrophobic
interactions between helix A and residues of β-catenin. The
color scheme is the same as Figure 1B, with β-catenin arm
repeats 11 and 12 termed R11 and R12, respectively. Side chains
from each protein that participate in hydrophobic interactions
are shown. Also shown is the superposition of the region II
helix of E-cadherin (Huber and Weis, 2001) (yellow; residue
numbers shown in parentheses). The superposition was performed
as described in Figure 1C. The hydrogen bond between Tyr 654 of
β-catenin and Asp 665 of E-cadherin is shown with a solid
line.(C) Electrostatic interactions (dashed lines) of ICAT
glutamate residues 37, 38, and 39 with arginine residues in
β-catenin or within ICAT, labeled as in (B). Mutation of these
three residues to alanine abolishes ICAT binding to β-catenin.
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