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Figure 3.
Figure 3. The Interactions between β-Catenin and the β
Strand in the Extended Region of XTcf3-CBD(A) Stereo
2F[o]−F[c] simulated annealed omit map of XTcf3-CBD. XTcf3
residues are denoted in yellow and β-catenin residues are
denoted in red. Solvent molecules are shown in turquoise. The
map is shown at a level of 1σ.(B) Structure of the XTcf3
extended region on the top of the β-catenin molecular surface.
Two semi-buried charged buttons, Lys-435 and Lys-312, are
critical for the β-catenin/Tcf interactions. The β-catenin
surface was cut off in the upper part of the figure to be able
to view the extended region of XTcf3-CBD. XTcf3 residues are
shown in white and exposed β-catenin residues due to the cut
surface are shown in green. XTcf3 residues are labeled in yellow
and β-catenin residues are labeled in white. The equipotential
contours at the relative levels of 10, 20, 30, 40, and 50 were
calculated with GRASP and are shown in white.(C) XTcf3 extended
region bonding diagram. The same conventions are used as in
Figure 2B.
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