Figure 1.
Figure 1. Structure of the Tcf4 - -catenin
complex. a, The Tcf4 peptide (yellow) has two sites of
interaction with the armadillo repeat region of -catenin
(blue): an 'extended region' composed of residues 13 -25
(labeled N in yellow) and a more C-terminal helical region
composed of residues 40 -50 (labeled C in yellow). The
intervening 14 residues are disordered, as are residues 8 -12 at
the N-terminus and 51 -54 at the C-terminus. b, Detail of
interactions in the extended region. Tcf4 residues Asp 16 and
Glu 17 form salt bridge hydrogen bonds with -catenin
Lys 435 and Lys 508, respectively. For clarity, only a subset of
the hydrogen bonds in this region is indicated. c, Detail of
interactions in the C-terminal helix. Tcf4 residues Leu 41, Val
44, Leu 48 and Val 49 form the hydrophobic surface of the
amphipathic helix. In (b,c), Tcf4 residues are colored yellow
and -catenin
residues are shown in blue. Thin magenta lines indicate hydrogen
bonds; the small red sphere is an ordered water molecule. The
figure was prepared with MOLSCRIPT33.
-catenin
complex. a, The Tcf4 peptide (yellow) has two sites of
interaction with the armadillo repeat region of 
-catenin
(blue): an 'extended region' composed of residues 13 -25
(labeled N in yellow) and a more C-terminal helical region
composed of residues 40 -50 (labeled C in yellow). The
intervening 14 residues are disordered, as are residues 8 -12 at
the N-terminus and 51 -54 at the C-terminus. b, Detail of
interactions in the extended region. Tcf4 residues Asp 16 and
Glu 17 form salt bridge hydrogen bonds with