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Figure 4.
Figure 4. Interaction of α- and β-Catenin in βα-cat(A)
Superdex 75 gel filtration chromatography of α-cat 57–264 and
βα-cat. Peak fractions were analyzed by SDS-PAGE and Coomassie
blue staining. The estimated molecular weight for the two peaks
is indicated.(B) Ribbon diagram of the chimera βα-cat. The
color scheme is the same as in the schematic of the model
(Figure 3). Residues 82–261, corresponding to the α-cat
82–279 protomer structure, are in yellow; residues 57–81 of
α-catenin are in blue; the β-catenin sequence is in red. The
flexible glycine linker between β- and α-catenin, which is not
visible in the structure, is shown as a dashed green line; the N
and C termini of the α-catenin and the β-catenin fragment are
indicated.(C) Contacts formed by tyrosine 142. View of tyrosine
142 in the βα-cat structure. The color scheme is the same as
for the βα-cat structure. Amino acids interacting with
tyrosine 142 are shown in ball and stick representation. Carbon,
nitrogen, and oxygen atoms are shown as gray, blue, and red
spheres, respectively. α and β indicate that these amino acids
belong to α-catenin and β-catenin, respectively. Nonpolar van
der Waals contacts are indicated by thin lines; hydrogen bonds
are shown as thin, dashed lines.
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