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@ARTICLE{Hofmann:49408,
      author       = {Hofmann, G. and Schweimer, K. and Kiessling, A. and
                      Hofinger, E. and Bauer, F. and Hoffmann, S. and Rosch, P.
                      and Campbell, I. D. and Werner, J. M. and Sticht, H.},
      title        = {{B}inding, domain orientation, and dynamics of the {L}ck
                      {SH}3-{SH}2 domain pair and comparison with other
                      {S}rc-family kinases},
      journal      = {Biochemistry},
      volume       = {44},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-49408},
      pages        = {13043 - 13050},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The catalytic activity of Src-family kinases is regulated
                      by association with its SH3 and SH2 domains. Activation
                      requires displacement of intermolecular contacts by SH3/SH2
                      binding ligands resulting in dissociation of the SH3 and SH2
                      domains from the kinase domain. To understand the
                      contribution of the SH3-SH2 domain pair to this regulatory
                      process, the binding of peptides derived from
                      physiologically relevant SH2 and SH3 interaction partners
                      was studied for Lck and its relative Fyn by NMR
                      spectroscopy. In contrast to Fyn, activating ligands do not
                      induce communication between SH2 and SH3 domains in Lck.
                      This can be attributed to the particular properties of the
                      Lck SH3-SH2 linker which is shown to be extremely flexible
                      thus effectively decoupling the behavior of the SH3 and SH2
                      domains. Measurements on the SH32 tandem from Lck further
                      revealed a relative domain orientation that is distinctly
                      different from that found in the Lck SH32 crystal structure
                      and in other Src kinases. These data suggest that
                      flexibility between SH2 and SH3 domains contributes to the
                      adaptation of Src-family kinases to specific environments
                      and distinct functions.},
      keywords     = {Humans / Ligands / Lymphocyte Specific Protein Tyrosine
                      Kinase p56(lck): chemistry / Lymphocyte Specific Protein
                      Tyrosine Kinase p56(lck): metabolism / Nuclear Magnetic
                      Resonance, Biomolecular / Peptides: metabolism / Protein
                      Binding / Protein Structure, Tertiary / Proto-Oncogene
                      Proteins c-fyn: chemistry / src Homology Domains /
                      src-Family Kinases: chemistry / Ligands (NLM Chemicals) /
                      Peptides (NLM Chemicals) / FYN protein, human (NLM
                      Chemicals) / Lymphocyte Specific Protein Tyrosine Kinase
                      p56(lck) (NLM Chemicals) / Proto-Oncogene Proteins c-fyn
                      (NLM Chemicals) / src-Family Kinases (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:16185072},
      UT           = {WOS:000232253700013},
      doi          = {10.1021/bi050814y},
      url          = {https://juser.fz-juelich.de/record/49408},
}