Acquisition of high-affinity, SH2-targeted ligands via a spatially focused library [2]

Journal of Medicinal Chemistry

Volumn 42, Issue 5, 1999, Pages 784-787

  Lee, Tae Ryong ^a   Lawrence, David S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; PHOSPHOTYROSINE; PROTEIN KINASE P60;

ACYLATION; BINDING AFFINITY; BINDING SITE; DISULFIDE BOND; LETTER; LIGAND BINDING; PEPTIDE SYNTHESIS; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

BENZENE DERIVATIVES; COUMARINS; ENZYME-LINKED IMMUNOSORBENT ASSAY; LIGANDS; MODELS, MOLECULAR; OLIGOPEPTIDES; SRC HOMOLOGY DOMAINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0001258839     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm980663f     Document Type: Letter

References (29)

1. The Src tyrosine kinase and members of the Src enzyme subfamily are modular proteins containing two types of protein-protein interaction domains (SH2 and SH3) as well as an active site region. The Src kinase itself was first identified in Rous sarcoma virus-infected chicken fibroblasts. Subsequently, a number of other closely related tyrosine kinases were reported, including Lck (Lymphoid T cell tyrosine kinase) and Fyn (named as a consequence of its homology to two other Src-related enzymes, Fgr and Yes). The abbreviations for the other SH2 domain-containing proteins in this study include PLC (phospholipase C), PI3 kinase (phosphatidylinositol-3-kinase), and Grb2 (growth factor receptor-bound protein 2).
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