|
Figure 1.
Solution structure of Par-3 PDZ3. A, stereoview showing the
backbones of 20 superimposed NMR-derived structures of Par-3
PDZ3. B, ribbon diagram of a representative NMR structure of the
Par-3 PDZ3. The secondary structure elements of PDZ3 are labeled
according to the scheme used for the canonic PDZ domains. The
potential peptide binding pocket is highlighted by a magenta
oval. C, amino acid sequence alignment of the Par-3 PDZ3 from
different species. The highly conserved hydrophobic, positively
charged, and negatively charged residues are in yellow, blue,
and red, respectively; other highly conserved residues are in
green. The secondary structures of Par-3 PDZ3 and the residue
number are marked at the top of the alignment. The positively
charged residues responsible for the specific charge-charge
interaction between PDZ3 and the PTEN peptide are highlighted by
blue triangles. The protein structure figures were prepared
using the programs MOLMOL (45), MOLSCRIPT (46), PyMOL (available
on the World Wide Web), and GRASP (47).
|
