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@ARTICLE{Bauer:46280,
      author       = {Bauer, F. and Hofinger, E. and Hoffmann, S. and Rösch, P.
                      and Schweimer, K. and Sticht, H.},
      title        = {{C}haracterization of {L}ck-binding elements in the
                      herpesviral regulatory {T}ip protein},
      journal      = {Biochemistry},
      volume       = {43},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-46280},
      pages        = {14932-9},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Herpesvirus saimiri encodes a tyrosine kinase interacting
                      protein (Tip) that binds to T-cell-specific tyrosine kinase
                      Lck via multiple sequence motifs and controls its activity.
                      The regulation of Lck by Tip represents a key mechanism in
                      the transformation of human T-lymphocytes during herpesviral
                      infection. In this study, the interaction of Tip with the
                      regulatory SH3 and SH2 domains of Lck was investigated by
                      biophysical and computational techniques. NMR spectroscopy
                      of isotopically labeled Tip(140-191) revealed that the
                      interaction with the LckSH3 domain is not restricted to the
                      classical proline-rich motif, but also involves the
                      C-terminally adjacent residues which pack into a hydrophobic
                      pocket on the surface of the SH3 domain, thus playing a
                      likely role in mediating binding specificity. Fluorescence
                      binding studies of Tip further demonstrate that Tyr127 in
                      its phosphorylated form represents a strong ligand of the
                      LckSH2 domain, indicating the presence of an additional Lck
                      interaction motif. In contrast, Tyr114, known to be
                      essential for STAT-3 binding, does not interact with the
                      LckSH2 domain, showing that the tyrosines in Tip exhibit
                      distinct binding specificity. The existence of numerous
                      interaction sites between Tip and the regulatory domains of
                      Lck implies a complex regulatory mechanism and may have
                      evolved to allow a gradual regulation of Lck activity in
                      different pathogenic states.},
      keywords     = {Amino Acid Sequence / Circular Dichroism / Cloning,
                      Molecular / Conserved Sequence / Herpesvirus 2, Saimiriine:
                      chemistry / Herpesvirus 2, Saimiriine: enzymology /
                      Herpesvirus 2, Saimiriine: metabolism / Hydrophobic and
                      Hydrophilic Interactions / Kinetics / Ligands / Lymphocyte
                      Specific Protein Tyrosine Kinase p56(lck): chemistry /
                      Lymphocyte Specific Protein Tyrosine Kinase p56(lck):
                      metabolism / Models, Molecular / Molecular Sequence Data /
                      Nuclear Magnetic Resonance, Biomolecular / Phosphoproteins:
                      chemistry / Phosphoproteins: genetics / Phosphoproteins:
                      isolation $\&$ purification / Phosphoproteins: metabolism /
                      Phosphotyrosine: chemistry / Protein Binding / Protein
                      Structure, Secondary / Protons / Sequence Homology, Amino
                      Acid / Spectrometry, Fluorescence / Viral Proteins:
                      chemistry / Viral Proteins: genetics / Viral Proteins:
                      isolation $\&$ purification / Viral Proteins: metabolism /
                      Ligands (NLM Chemicals) / Phosphoproteins (NLM Chemicals) /
                      Protons (NLM Chemicals) / Viral Proteins (NLM Chemicals) /
                      tyrosine kinase interacting protein, Saimiriine herpesvirus
                      2 (NLM Chemicals) / Phosphotyrosine (NLM Chemicals) /
                      Lymphocyte Specific Protein Tyrosine Kinase p56(lck) (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15554700},
      UT           = {WOS:000225353300007},
      doi          = {10.1021/bi0485068},
      url          = {https://juser.fz-juelich.de/record/46280},
}