N-myristoylation of a peptide substrate for Src converts it into an apparent slow-binding bisubstrate-type inhibitor

Journal of Peptide Research

Volumn 53, Issue 5, 1999, Pages 569-577

  Ramdas, L ^a   Obeyesekere, N U ^a   Sun, G ^a   McMurray, J S ^a   Budde, R J A ^a  

^a UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

Author keywords

Acylated peptides; Bisubstrate inhibitors; Myristoylation; PTK inhibitors; Src

Indexed keywords

PROTEIN TYROSINE KINASE;

ARTICLE; CELL TRANSFORMATION; ENZYME SUBSTRATE COMPLEX; MYRISTYLATION; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

ACYLATION; DRUG DESIGN; ENZYME INHIBITORS; LIPOPROTEINS; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS PP60(C-SRC); RECEPTORS, FIBROBLAST GROWTH FACTOR; RECOMBINANT FUSION PROTEINS; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0032996933     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00063.x     Document Type: Article

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