Src homology-2 domains: Structure, mechanisms, and drug discovery
- 12 December 1998
- journal article
- review article
- Published by Wiley in Biopolymers
- Vol. 47 (3) , 243-261
- https://doi.org/10.1002/(sici)1097-0282(1998)47:3<243::aid-bip4>3.0.co;2-p
Abstract
Src homology‐2 (SH2) domains and their associated catalytic or noncatalytic proteins constitute critical signal transduction targets for drug discovery. Such SH2 proteins are found in the regulation of a number of cellular processes, including growth, mitogenesis, motility, metabolism, immune response, and gene transcription. From the relationship of tyrosine phosphorylation and intracellular regulation by protein–tyrosine kinases (PTKs) and protein–tyrosine phosphatases (PTPs), the dynamic and reversible binding interactions of SH2 domain containing proteins with their cognate phosphotyrosine (pTyr) containing proteins provide a third dimensionality to the orchestration of signal transduction pathways that exist as a result of pTyr formation, degradation, and molecular recognition events. This review highlights several key research achievements impacting our current understanding of SH2 structure, mechanisms, and drug discovery that underlie the role(s) of SH2 domains in signal transduction processes, cellular functions, and disease states. © 1998 John Wiley & Sons, Inc. Biopoly 47: 243–261, 1998Keywords
This publication has 37 references indexed in Scilit:
- Structure-Based Design of a Novel Series of Nonpeptide Ligands That Bind to the pp60src SH2 DomainJournal of the American Chemical Society, 1997
- Non-peptide itam mimics as ZAP-70 antagonistsBioorganic & Medicinal Chemistry Letters, 1997
- CELLULAR FUNCTIONS REGULATED BY SRC FAMILY KINASESAnnual Review of Cell and Developmental Biology, 1997
- Design, Synthesis, and Cocrystal Structure of a Nonpeptide Src SH2 Domain LigandJournal of Medicinal Chemistry, 1997
- The Role of 4-phosphonodifluoromethyl- and 4-phosphono-phenylalanine in the selectivity and cellular uptake of SH2 domain ligandsBioorganic & Medicinal Chemistry Letters, 1997
- Solution structure of the C-terminal SH2 domain of the human tyrosine kinase Syk complexed with a phosphotyrosine pentapeptideStructure, 1995
- Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptorNature, 1995
- Potent Inhibition of Insulin Receptor Dephosphorylation by a Hexamer Peptide Containing the Phosphotyrosyl Mimetic F2PmpBiochemical and Biophysical Research Communications, 1994
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993
- Three-dimensional solution structure of the src homology 2 domain of c-ablCell, 1992