Bioorganic Chemistry of Biological Signal Transduction by Alexander Levitzki (auth.), Prof. Dr. Herbert Waldmann

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 focusing 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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Reminiscent of the covalent inhibition principle employed by Glaxo with 33 (Scheme 5), AP22161 64 covalently binds to the target SH2 domain. 24 µmol/l against the Src SH2 domain, it was also shown in vivo to diminish the osteoclast resorption activity in a mechanism-based cellular assay [161]. , the ZAP70 SH2 domain [162]. Again the lead finding efficiency was significantly increased by developing privileged peptidomimetic building blocks that account for the target family-wide mole- Peptidomimetic SH2 Domain Antagonists for Targeting Signal Transduction 49 cular recognition characteristics, followed by a repeated use of these modules in different medicinal chemistry programs.

Pdb). The Asn-Pro-Ala-pTyr tetrapeptide sequence adopts a regular bI turn conformation [181] Peptidomimetic SH2 Domain Antagonists for Targeting Signal Transduction 53 Although PTB domains and SH2 domains are both capable of phosphorylation-dependent binding [177], their ligand “read-out” and binding modes are substantially different. Specificity on PTB domain interaction is conferred by sequences N-terminal to pTyr (Fig. 12), rather than C-terminal as found for SH2 domains. PTB domains were identified based on their ability to recognize and bind -Asn-Pro-Any-pTyr- sequences [178].

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