Figure 2 - full size

 

Figure 2.
Figure 2. The Pin1 -CTD peptide binding interface. a, Ribbon diagram of the Pin1 WW domain bound to Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser depicted after a 90 rotation around a vertical axis from the view shown in Fig. 1a. This view is looking onto the concave WW domain peptide binding surface opposite the PPIase domain. The carbon atoms of the CTD peptide are colored gold to distinguish them from the WW domain side chain atoms. The water molecule mediating Tyr 23 -phosphate contacts is shown as a cyan sphere. Hydrogen bonds are shown as green dotted spheres. b, Molecular surface representation of the WW domain -peptide interface rendered after a slight rotation around the vertical axis from the view depicted in (a). The solvent accessible surface for the Pin1 WW domain residues was calculated in GRASP33, and the acidic and basic residues colored red and blue, respectively. c, Schematic and energetic view of the Pin1 -phosphopeptide complex. Pin1 residues are purple and CTD residues black. Residues participating in van der Waals contacts are highlighted with gold and the extended van der Waals surfaces appear as dotted gold curves. Hydrogen bonds are shown as dashed green lines. In the case of the S16H and W34H mutants, some of the apparent binding is likely being contributed by the PPIase domain. Residues are given in the single letter code. Values in parentheses represent deviations from theoretical binding isotherms.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 639-643) copyright 2000.