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Figure 4.
Figure 4. (a) Surface representation of the FE65 WW bound to
the Mn10 peptide (shown as a stick model). Semitransparent
rectangles denote the parallel orientation of the XP and XP2
grooves. (b) A diagram of the FE65 WW bound to Mn10 PPII helix
(shown as a triangular prism), illustrating the parallel
arrangement of the XP and XP2 grooves, the three aromatic
residues that form them, and the proline residues of the ligand
that occupy them (orange spheres). Unbound proline and leucine
residues are shown as gray and cyan spheres, respectively. (c)
Surface representation of the FBP11 WW1 bound to PPLP sequence
(PDB code 2DYF), showing the non-parallel arrangement of the XP
and XP2 grooves (rectangles). (d) Surface representation of the
Abl tyrosine kinase SH3 domain bound to the peptide 3BP1
containing the sequence PPLPP (PDB code 1ABO), showing the
parallel XP and XP2 grooves (rectangles). (e) A stereo view of
the FE65 WW–Mn10 structure superimposed on the Abl SH3–3BP1
complex, showing the similar mode of PPII recognition by the
aromatic triad of WW (yellow) and SH3 (light green) domains. The
Mn10 and 3BP1 peptides are shown in cyan and pink, respectively.
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