Figure 2.
Figure 2. Comparison of the structural conformations of hTcf4
and XTcf3 near the second charged button (Lys 312). Stick
models of the central region of the a, hTcf4-CBD and b,
XTcf3-CBD on top of the -catenin
molecular surface, which has been shaded to denote the basic
(blue) and acidic (red) regions. The Tcf Glu residues are
color-coded as in Fig. 1b. This figure was generated by GRASP27.
c, Bonding diagram of the hTcf4-CBD kinked helical region. The
hTcf4 residues are shown in black; -catenin
residues, in red. Hydrophobic interactions are denoted by a red
starburst, and hydrogen bonds and charged interactions are
denoted in green. Solvent molecules are shown in turquoise. d,
Stereo 2F[o] - F[c] omit map of hTcf4-CBD. The hTcf4 residues
are denoted in yellow; the -catenin
residues, in red. The map is contoured at 1 .
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2001,
8,
1048-1052)
copyright 2001.
-catenin
molecular surface, which has been shaded to denote the basic
(blue) and acidic (red) regions. The Tcf Glu residues are
color-coded as in Fig. 1b. This figure was generated by GRASP27.
c, Bonding diagram of the hTcf4-CBD kinked helical region. The
hTcf4 residues are shown in black; 
.