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Figure 3.
Figure 3 Tetraproline region and PPII helix-binding site of
VavS. (A) The ribbon diagram for VavS in the complex crystal is
shown with the tetraproline region close to the viewer. Residues
606 -612 encompassing the tetraproline region, and the residues
interacting with them or expected to form the PPII helix-binding
site are drawn as rods in red and blue, respectively. (B) The
molecular surface of VavS by GRASP (Nicholls et al., 1991) is
colored according to the local electrostatic potential, with
colors ranging from blue (positive) to red (negative) through
white (neutral). The tetraproline region is drawn as red rods,
and the peptide ligand for the Sem-5 SH3 domain is superposed on
the molecular surface (yellow rods). The expected binding sites
of VavS for the proline-rich peptide are labeled with their
identification codes.
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