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@ARTICLE{Tran:49405,
      author       = {Tran, T. and Hoffmann, S. and Wiesehan, K. and Jonas, E.
                      and Luge, C. and Aladag, A. and Willbold, D.},
      title        = {{I}nsights into {H}uman {L}ck {SH}3 {D}omain {B}inding
                      {S}pecificity: {D}ifferent {B}inding {M}odes of {A}rtificial
                      and {N}ative {L}igands},
      journal      = {Biochemistry},
      volume       = {44},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-49405},
      pages        = {15042 - 15052},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We analyzed the ligand binding specificity of the
                      lymphocyte specific kinase (Lck) SH3 domain. We identified
                      artificial Lck SH3 ligands using phage display. In addition,
                      we analyzed Lck SH3 binding sites within known natural Lck
                      SH3 binding proteins using an Lck specific binding assay on
                      membrane-immobilized synthetic peptides. On one hand, from
                      the phage-selected peptides, representing mostly special
                      class I' ligands, a well-defined consensus sequence was
                      obtained. Interestingly, a histidine outside the central
                      polyproline motif contributes significantly to Lck SH3
                      binding affinity and specificity. On the other hand, we
                      confirmed previously mapped Lck SH3 binding sites in ADAM15,
                      HS1, SLP76, and NS5A, and identified putative Lck SH3
                      binding sites of Sam68, FasL, c-Cbl, and Cbl-b. Without
                      exception, the comparatively diverse Lck SH3 binding sites
                      of all analyzed natural Lck SH3 binding proteins emerged as
                      class II proteins. Possible explanations for the observed
                      variations between artificial and native ligands-which are
                      not due to significant K(D) value differences as shown by
                      calculating Lck SH3 affinities of artificial peptide
                      PD1-Y(-3)R as well as for peptides comprising putative Lck
                      SH3 binding sites of NS5A, Sos, and Sam68-are discussed. Our
                      data suggest that phage display, a popular tool for
                      determining SH3 binding specificity, must-at least in the
                      case of Lck-not irrevocably mirror physiologically relevant
                      protein-ligand interactions.},
      keywords     = {Amino Acid Sequence / Binding Sites / Consensus Sequence /
                      Histidine: chemistry / Humans / Ligands / Lymphocyte
                      Specific Protein Tyrosine Kinase p56(lck): chemistry /
                      Lymphocyte Specific Protein Tyrosine Kinase p56(lck):
                      metabolism / Peptide Library / Peptides: chemistry / Protein
                      Binding / Sequence Alignment / Tyrosine: chemistry / src
                      Homology Domains / Ligands (NLM Chemicals) / Peptide Library
                      (NLM Chemicals) / Peptides (NLM Chemicals) / Tyrosine (NLM
                      Chemicals) / Histidine (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:16274251},
      UT           = {WOS:000233295900036},
      doi          = {10.1021/bi051403k},
      url          = {https://juser.fz-juelich.de/record/49405},
}