Visualizing the Induced Binding of SH2-Phosphopeptide (Articolo in rivista)

Type
Label
  • Visualizing the Induced Binding of SH2-Phosphopeptide (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/ct300003f (literal)
Alternative label
  • Giorgino, T.;Buch, I.;de Fabritiis, G. (2012)
    Visualizing the Induced Binding of SH2-Phosphopeptide
    in Journal of chemical theory and computation
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giorgino, T.;Buch, I.;de Fabritiis, G. (literal)
Pagina inizio
  • 1171 (literal)
Pagina fine
  • 1175 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://pubs.acs.org/doi/abs/10.1021/ct300003f (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 8 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 4 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1: Institute of Biomedical Engineering, CNR - National Research Council of Italy, Corso Stati Uniti 4, 35127 Padova, Italy / 2, 3: +Computational Biochemistry and Biophysics Laboratory (GRIB-IMIM), Universitat Pompeu Fabra, Barcelona Biomedical Research Park, C/Dr. Aiguader 88, 08003 Barcelona, Spain (literal)
Titolo
  • Visualizing the Induced Binding of SH2-Phosphopeptide (literal)
Abstract
  • Approximately 100 proteins in the human genome contain an SH2 domain recognizing small flexible phosphopeptides. It is therefore important to understand in atomistic detail the way these peptides bind and the conformational changes that take place upon binding. Here, we obtained several spontaneous binding events between the p56 lck SH2 domain and the pYEEI peptide within 2 Å RMSD from the crystal structure and with kinetic rates compatible with experiments using high-throughput molecular dynamics simulations. Binding is achieved in two phases, fast contacts of the charged phospho-tyrosine and then rearrangement of the ligand involving the stabilization of two important loops in the SH2 domain. These observations provide insights into the binding pathways and induced conformations of the SH2-phosphopeptide complex which, due to the characteristics of SH2 domains, should be relevant for other SH2 recognition peptides (literal)
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