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• W2051269710 endingPage "130" @default.
• W2051269710 startingPage "124" @default.
• W2051269710 abstract "A series of 48 cyclic peptides based on the amino acid sequence surrounding the autophosphorylation site of pp60c-srcwas synthesized and each was tested as both a substrate and an inhibitor of this protein tyrosine kinase. Starting with cyclo(Asp1-Asn2-Gln3-Tyr4-Ala5-Ala6-Arg7-Gln8-d-Phe9-Pro10) a six-amino-acid survey was performed at positions 1 through 8 to determine which positions were critical for affinity and phosphorylation and which amino acids produced the greatest activity. Our survey found that Arg7was detrimental for binding and phosphorylation and that aromatic residues were preferred at this position. Further increases in affinity were obtained with hydrophobic residues at position 6 with the optimum for both affinity and phosphorylation being Phe. Changes on the “amino-terminal” side of Tyr4resulted in reducedVmaxvalues, illustrating the requirement for acidic residues in peptidic tyrosine kinase substrates. The result of the survey was cyclo(Asp1-Asn2-Gln3-Tyr4-Ala5-Phe6-Phe7-Gln8-d-Phe9-Pro10). The change of residues 6 and 7 resulted in a 42-fold increase in affinity and no increase inVmax. As a substrate, this peptide displayed Michaelis–Menten kinetics at saturating ATP conditions. As an inhibitor, mixed inhibition was observed. A linear version of this peptide was 13-fold less potent an inhibitor than the cyclic peptide." @default.
• W2051269710 created "2016-06-24" @default.
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• W2051269710 date "1998-07-01" @default.
• W2051269710 modified "2023-10-16" @default.
• W2051269710 title "Cyclic Peptides as Probes of the Substrate Binding Site of the Cytosolic Tyrosine Kinase, pp60c-src" @default.
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• W2051269710 doi "https://doi.org/10.1006/abbi.1998.0707" @default.
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