By Alexander Levitzki (auth.), Prof. Dr. Herbert Waldmann (eds.)
A. Levitzki: Protein Tyrosine Kinase Inhibitors As healing Agents.- G. Müller: Peptiddomimetic SH2 area Antagonists for concentrating on sign Transduction.- J. Kuhlmann and C. Herrmann: Biophysical Characterisation of the Ras Protein.- H. Waldmann and M. Thutewohl: Ras-Farnesyltransferase-Inhibitors As Promising Anti-Tumor Drugs.- P.J. Hergenrother and S.F. Martin: Phosphatidylcholine-Preferring Phospholipase C from B. cereus. functionality, constitution and Mechanism.- G. Dormán: Photoaffinity Labeling in organic sign Transduction.
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Org/pdb/) contains around 80 entries of SH2 domain structures and complexes thereof. Today, the SH2 domain structures of Hck [62], Src [63–66], Abl [67], Grb2 [68–71], Syp [72], PLCg [73], Fyn [74], SAP [75], Lck [76, 77], the C- and N-terminal SH2 domain of p85a [78–80], and of the tandem SH2 domains Syk [81, 82], ZAP70 [83, 84], and SHP-2 [85] are determined. All SH2 domains display a conserved 3D structure as can be expected from multiple sequence alignments (Fig. 4). The common structural fold consists of a central three-stranded antiparallel b sheet that is occasionally extended by one to three additional short strands (Fig.
1). SH2 domains specifically recognize phosphorylated tyrosine (pTyr) residues on cytoplasmic receptor domains or soluble signaling components [49–51]. The pTyr-flanking amino acid residues constitute the SH2 domain docking site and determine which SH2-containing signaling proteins associate with the phosphorylated protein surface [52–56]. , a single cytoplasmic receptor domain can recruit numerous different SH2 domain proteins as exemplified for the PDGF (platelet-derived growth factor) receptor (Fig.
7 and 8). , isothermal titration calorimetry revealed the “two-pronged plug – twoholed socket” model to be an oversimplification of the details underlying the true binding mechanism [86–97]. No significant differences within the specific thermodynamic signature were detected for binding of different peptides with altered sidechains of variable size and hydrophobicity at the pTyr+3 position. 28 G. Müller Fig. 7. PDB). The protein is shown as a ribbon diagram, while the ligand binding site is highlighted by a Connolly surface in line-mode.