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@ARTICLE{BatraSafferling:9746,
      author       = {Batra-Safferling, R. and Granzin, J. and Moedder, S. and
                      Hoffmann, S. and Willbold, D.},
      title        = {{S}tructural studies of {PI}3{K} {SH}3 domain in complex
                      with a peptide ligand: role of anchor residue in ligand
                      binding},
      journal      = {Biological chemistry},
      volume       = {391},
      issn         = {1431-6730},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {PreJuSER-9746},
      pages        = {33 - 42},
      year         = {2010},
      note         = {The authors wish to thank Georg Buldt for continuous
                      generous support. Furthermore, technical assistance by
                      Esther Jonas and the beamline scientists at the ESRF
                      (Grenoble, France) is acknowledged. We also thank Oliver
                      Weiergraber for critical reading of the manuscript. This
                      work was supported by a grant from the Deutsche
                      Forschungsgemeinschaft (SFB 575, B11) to D.W.},
      abstract     = {Src homology 3 (SH3) domains are mediators of
                      protein-protein interactions. They comprise approximately 60
                      amino acid residues and are found in many intracellular
                      signaling proteins. Here, we present the crystal structure
                      of the SH3 domain from phosphatidylinositol 3-kinase (PI3K)
                      in complex with the 12-residue proline-rich peptide PD1R
                      (HSKRPLPPLPSL). The crystal structure of the PI3K SH3-PD1R
                      complex at a resolution of 1.7 A reveals type I ligand
                      orientation of the bound peptide with an extended
                      conformation where the central portion forms a left-handed
                      type II polyproline (PPII) helix. The overall structure of
                      the SH3 domain shows minimal changes on ligand binding. In
                      addition, we also attempted crystallization with another
                      peptide ligand (PD1) where the residue at anchor position
                      P(-3) is a tyrosine. The crystals obtained did not contain
                      the PD1 ligand; instead, the ligand binding site is
                      partially occupied by residues Arg18 and Trp55 from the
                      symmetry-related PI3K SH3 molecule. Considering these
                      crystal structures of PI3K SH3 together with published
                      reports, we provide a comparative analysis of protein-ligand
                      interactions that has helped us identify the individual
                      residues which play an important role in defining target
                      specificity.},
      keywords     = {Amino Acid Sequence / Binding Sites / Crystallography,
                      X-Ray / Ligands / Models, Molecular / Molecular Sequence
                      Data / Oligopeptides: metabolism / Peptides: chemistry /
                      Phosphatidylinositol 3-Kinases: chemistry /
                      Phosphatidylinositol 3-Kinases: metabolism / Protein Binding
                      / src Homology Domains: physiology / Ligands (NLM Chemicals)
                      / Oligopeptides (NLM Chemicals) / Peptides (NLM Chemicals) /
                      histidyl-seryl-lysyl-arginyl-prolyl-leucyl-prolyl-prolyl-leucyl-prolyl-seryl-leucine
                      (NLM Chemicals) / polyproline (NLM Chemicals) /
                      Phosphatidylinositol 3-Kinases (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-3 / ISB-2 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB942 / I:(DE-Juel1)ISB-2-20090406 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19919182},
      UT           = {WOS:000273206000004},
      doi          = {10.1515/bc.2010.003},
      url          = {https://juser.fz-juelich.de/record/9746},
}