Figure 4.

Mapping of detected phosphorylation sites to known structures. Peptides detected in the Bodenmiller analysis were mapped to highly similar, known structures. The three-dimensional structures are shown in orange spacefilling representation except where the peptides map to the structures (shown as black ribbons). Detected phosphorylation sites are shown as black dots. (a) The alternative isoforms generated from shaggy are 76% sequence identical to human glycogen synthase kinase 3 beta [PDB:1j1c]. The peptides detected in the analysis covered two regions. The amino-terminal region includes 22 residues that are known to be disordered in solution and are therefore not shown. (b) The structure for Drosophila fructose-1-biphosphate aldolase has been solved and the Bodenmiller analysis finds peptides covering two regions - both are on the surface of the structure. (c) Drosophila moesin has 75% identity to fall army worm moesin, for which the three-dimensional structure has been solved [PDB:2i1j]; in addition to the residues marked as found in the Bodenmiller analysis, a further 15 residues that were detected are not shown in the figure because they are disordered in solution. (d) The isoforms generated from alphabet are 52% identical to human phosphatase 2C [PDB:1a6q]. The analysis detected two peptides, one of which also coincided with the 14 disordered carboxy-terminal residues of the template (not shown).