% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Bauer:49418,
      author       = {Bauer, F. and Schweimer, K. and Meiselbach, H. and
                      Hoffmann, S. and Rosch, P. and Sticht, H.},
      title        = {{S}tructural characterization of {L}yn-{SH}3 domain in
                      complex with a herpesviral protein reveals an extended
                      recognition motif that enhances binding affinity},
      journal      = {Protein science},
      volume       = {14},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PreJuSER-49418},
      pages        = {2487 -2498},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The Src homology 3 (SH3) domain of the Src family kinase
                      Lyn binds to the herpesviral tyrosine kinase interacting
                      protein (Tip) more than one order of magnitude stronger than
                      other closely related members of the Src family. In order to
                      identify the molecular basis for high-affinity binding, the
                      structure of free and Tip-bound Lyn-SH3 was determined by
                      NMR spectroscopy. Tip forms additional contacts outside its
                      classical proline-rich recognition motif and, in particular,
                      a strictly conserved leucine (L186) of the C-terminally
                      adjacent sequence stretch packs into a hydrophobic pocket on
                      the Lyn surface. Although the existence of this pocket is no
                      unique property of Lyn-SH3, Lyn is the only Src family
                      kinase that contains an additional aromatic residue (H41) in
                      the n-Src loop as part of this pocket. H41 covers L186 of
                      Tip by forming tight hydrophobic contacts, and model
                      calculations suggest that the increase in binding affinity
                      compared with other SH3 domains can mainly be attributed to
                      these additional interactions. These findings indicate that
                      this pocket can mediate specificity even between otherwise
                      closely related SH3 domains.},
      keywords     = {Models, Molecular / Multiprotein Complexes: chemistry /
                      Multiprotein Complexes: metabolism / Nuclear Magnetic
                      Resonance, Biomolecular: methods / Phosphoproteins:
                      chemistry / Phosphoproteins: metabolism / Protein Binding /
                      Protein Structure, Quaternary / Viral Proteins: chemistry /
                      Viral Proteins: metabolism / src Homology Domains /
                      src-Family Kinases: chemistry / src-Family Kinases:
                      metabolism / Multiprotein Complexes (NLM Chemicals) /
                      Phosphoproteins (NLM Chemicals) / Viral Proteins (NLM
                      Chemicals) / tyrosine kinase interacting protein, Saimiriine
                      herpesvirus 2 (NLM Chemicals) / lyn protein-tyrosine kinase
                      (NLM Chemicals) / src-Family Kinases (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16155203},
      pmc          = {pmc:PMC2253286},
      UT           = {WOS:000232233400001},
      doi          = {10.1110/ps.051563605},
      url          = {https://juser.fz-juelich.de/record/49418},
}