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@ARTICLE{Schmidt:55440,
      author       = {Schmidt, H. and Hoffmann, S. and Tran, T. and Stoldt, M.
                      and Stangler, T. and Wiesehan, K. and Willbold, D.},
      title        = {{S}olution structure of a {H}ck {SH}3 domain ligand complex
                      reveals novel interaction modes},
      journal      = {Journal of molecular biology},
      volume       = {365},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-55440},
      pages        = {1517 - 1532},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We studied the interaction of hematopoietic cell kinase SH3
                      domain (HckSH3) with an artificial 12-residue proline-rich
                      peptide PD1 (HSKYPLPPLPSL) identified as high affinity
                      ligand (K(D)=0.2 muM). PD1 shows an unusual ligand sequence
                      for SH3 binding in type I orientation because it lacks the
                      typical basic anchor residue at position P(-3), but instead
                      has a tyrosine residue at this position. A basic lysine
                      residue, however, is present at position P(-4). The solution
                      structure of the HckSH3:PD1 complex, which is the first
                      HckSH3 complex structure available, clearly reveals that the
                      P(-3) tyrosine residue of PD1 does not take the position of
                      the typical anchor residue but rather forms additional van
                      der Waals interactions with the HckSH3 RT loop. Instead,
                      lysine at position P(-4) of PD1 substitutes the function of
                      the P(-3) anchor residue. This finding expands the well
                      known ligand consensus sequence +xxPpxP by +xxxPpxP. Thus,
                      software tools like iSPOT fail to identify PD1 as a
                      high-affinity HckSH3 ligand so far. In addition, a short
                      antiparallel beta-sheet in the RT loop of HckSH3 is observed
                      upon PD1 binding. The structure of the HckSH3:PD1 complex
                      reveals novel features of SH3 ligand binding and yields new
                      insights into the structural basics of SH3-ligand
                      interactions. Consequences for computational prediction
                      tools adressing SH3-ligand interactions as well as the
                      biological relevance of our findings are discussed.},
      keywords     = {Amides / Amino Acid Sequence / Binding Sites / Deuterium
                      Oxide: metabolism / Half-Life / Humans / Kinetics / Ligands
                      / Models, Molecular / Molecular Sequence Data / Nuclear
                      Magnetic Resonance, Biomolecular / Peptide Mapping /
                      Peptides: chemistry / Peptides: metabolism / Protein Binding
                      / Proto-Oncogene Proteins c-hck: analysis / Proto-Oncogene
                      Proteins c-hck: chemistry / Proto-Oncogene Proteins c-hck:
                      metabolism / Protons / Solutions / Water: metabolism / src
                      Homology Domains / Amides (NLM Chemicals) / Ligands (NLM
                      Chemicals) / Peptides (NLM Chemicals) / Protons (NLM
                      Chemicals) / Solutions (NLM Chemicals) / Water (NLM
                      Chemicals) / Deuterium Oxide (NLM Chemicals) / HCK protein,
                      human (NLM Chemicals) / Proto-Oncogene Proteins c-hck (NLM
                      Chemicals) / J (WoSType)},
      cin          = {INB-2 / JARA-SIM},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17141806},
      UT           = {WOS:000243749600023},
      doi          = {10.1016/j.jmb.2006.11.013},
      url          = {https://juser.fz-juelich.de/record/55440},
}