Structure-based design of peptidomimetic antagonists of p56(lck) SH2 domain

Starting from the tetrapeptide Ac-pYEEI-NHMe and using a structure-based approach, we have designed and synthesised a peptidomimetic ligand for p56(lck) SH2 domain containing a conformationally restricted replacement for the two glutamate residues. We have explored replacments for the isoleucine res...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 2002-05, Vol.12 (10), p.1365-1369
Hauptverfasser:	Hobbs, Christopher J, Bit, Rino A, Cansfield, Andrew D, Harris, Bill, Hill, Christopher H, Hilyard, Katherine L, Kilford, Ian R, Kitas, Eric, Kroehn, Antonin, Lovell, Peter, Pole, David, Rugman, Paul, Sherborne, Brad S, Smith, Ian E D, Vesey, David R, Walmsley, D Lee, Whittaker, David, Williams, Glyn, Wilson, Fiona, Banner, David, Surgenor, Allan, Borkakoti, Neera
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cricetinae Crystallography, X-Ray Drug Design Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - pharmacology Glutamic Acid Ligands Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - antagonists & inhibitors Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - chemistry Models, Molecular Molecular Conformation Oligopeptides - chemical synthesis Oligopeptides - pharmacology src Homology Domains Structure-Activity Relationship
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