Figure 2.
FIGURE 2. Solution structure of Dkk2C. A, amino acid
sequence alignment of C-terminal cysteine-rich domains of Dkks
in mouse (m), human (h), Xenopus (x), rabbit (r), and zebrafish
(z).β strand elements identified in the three-dimensional
structure of Dkk2C are indicated at the top. Ten conserved
cysteines are in bold type, and pairs of cysteines forming
disulfide bridges are colored identically and linked by lines.
Amino acids that contact the third β-propeller domain of LRP5
in the docked model are in bold and indicated by the red dots.
B, stereo view of the peptide backbone (N, C- , C')
determined by superimposition of 20 conformers of Dkk2C with the
lowest target function values. The figure was generated by using
MOLMOL (39). β strands are red; disulfide bridges are yellow.
C, ribbon diagram of Dkk2C with the lowest target function
values, generated by using MOLSCRIPT (40).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2008,
283,
23364-23370)
copyright 2008.
, C')
determined by superimposition of 20 conformers of Dkk2C with the
lowest target function values. The figure was generated by using
MOLMOL (39). β strands are red; disulfide bridges are yellow.
C, ribbon diagram of Dkk2C with the lowest target function
values, generated by using MOLSCRIPT (40).