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Figure 2.
Figure 2. Interactions between the Extended Region of
Phospho-APC and β-Catenin(A) Electrostatic surface of
β-catenin (armadillo repeats 10-12) bound to the α-helix of
APC-2,3 (shown in stick form) N-terminal to the extended region.
The surface of β-catenin is colored according to its relative
electrostatic potential with blue representing positively
charged residues and red representing negatively charged
residues. β-catenin and APC amino acids are labeled in yellow
and red, respectively.(B) Electrostatic surface of β-catenin
(armadillo repeats 5-9) bound to the extended region of
phospho-APC.(C) Critical contacts in the interface between the
phospho-APC extended region and the β-catenin groove of
armadillo repeats 5-9. APC is shown in a red ball-and-stick
representation with red labels, and β-catenin (with helices
colored as in Figure 1B) side chains are yellow with black
labels. Phosphorylated Thr1487 of APC is labeled in italics. The
hydrogen bonding and charge-charge interactions are designated
with pink lines. Water molecules in the interface are shown as
blue balls. For clarity, hydrogen bonds bridged by water
molecules between APC and β-catenin residues, R474, R386, D390,
and K354, are not shown.
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