Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases. (Articolo in rivista)

Type
Label
  • Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases. (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jm051080q (literal)
Alternative label
  • Paolo Ruzza; Luca Cesaro; Dirk Tourwé; Andrea Calderan; Barbara Biondi; Veronique Maes; Ileana Menegazzo; Alessio Osler; Chiara Rubini; Andrea Guiotto; Lorenzo A. Pinna; Gianfranco Borin; Arianna Donella-Deana (2006)
    Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases.
    in Journal of medicinal chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Paolo Ruzza; Luca Cesaro; Dirk Tourwé; Andrea Calderan; Barbara Biondi; Veronique Maes; Ileana Menegazzo; Alessio Osler; Chiara Rubini; Andrea Guiotto; Lorenzo A. Pinna; Gianfranco Borin; Arianna Donella-Deana (literal)
Pagina inizio
  • 1916 (literal)
Pagina fine
  • 1924 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 49 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 6 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomolecular Chemistry of CNR, Padova Unit, Via F. Marzolo 1, 35131 Padova, Italy; Department of Biological Chemistry, University of Padova, Via G. Colombo 3, 35131 Padova, Italy; Vrije Universiteit Brussel, Organic Chemistry Department, Pleinlann 2, B-1050 Brussel, Belgium; Department of Chemical Sciences, University of Padova, Via F. Marzolo 1, 35131 Padova, Italy (literal)
Titolo
  • Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases. (literal)
Abstract
  • The side chain orientation of the tyrosine residue included in a peptide, which is an excellent substrate of Syk tyrosine kinase, was fixed in different conformations by either incorporating the tyrosine in cyclic structures (6-OH-Tic, 5-OH-Aic, and Hat derivatives) or adding a sterically bulky substituent in the tyrosine side chain moiety (beta-MeTyr). Synthetic peptides containing tyrosine analogues displaying different side chain orientations were analyzed by NMR techniques and tested as potential substrates of the nonreceptor tyrosine kinases Syk, Csk, Lyn, and Fyn. The \"rotamer scan\" of the phosphorylatable residue generated optimal substrates in terms of both phosphorylation efficiency and selectivity for Syk tyrosine kinase, while the peptidomimetics were not recognized by the other tyrosine kinases. In particular, L-beta-MeTyr and D-Hat containing peptides resulted to be both suitable substrates for the specific monitoring of Syk and consensus sequence scaffolds for the design of potential inhibitors highly selective for this tyrosine kinase. (literal)
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