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@ARTICLE{Thielmann:62893,
      author       = {Thielmann, Y. and Mohrlüder, J. and Koenig, B. W. and
                      Stangler, T. and Hartmann, R. and Becker, K. and Höltje,
                      H.-D. and Willbold, D.},
      title        = {{A}n indole binding site is a major determinant of the
                      ligand specificity of the {GABA} type {A}
                      receptor-associated protein {GABARAP}},
      journal      = {ChemBioChem},
      volume       = {9},
      issn         = {1439-4227},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {PreJuSER-62893},
      pages        = {1767 - 1775},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The role of tryptophan as a key residue for ligand binding
                      to the ubiquitin-like modifier GABA(A) receptor associated
                      protein (GABARAP) was investigated. Two tryptophan-binding
                      hydrophobic patches were identified on the conserved face of
                      the GABARAP structure by NMR spectroscopy and molecular
                      docking. GABARAP binding of indole and indole derivatives,
                      including the free amino acid tryptophan was quantified. The
                      two tryptophan binding sites can be clearly distinguished by
                      mapping the NMR spectroscopy-derived residue-specific
                      apparent dissociation constant, K(d), onto the
                      three-dimensional structure of GABARAP. The biological
                      relevance of tryptophan-binding pockets of GABARAP was
                      supported by a highly conserved tryptophan residue in the
                      GABARAP binding region of calreticulin, clathrin heavy
                      chain, and the gamma2 subunit of the GABA(A) receptor.
                      Replacement of tryptophan by alanine abolished ligand
                      binding to GABARAP.},
      keywords     = {Adaptor Proteins, Signal Transducing: chemistry / Adaptor
                      Proteins, Signal Transducing: metabolism / Amino Acid
                      Sequence / Animals / Binding Sites / Humans / Hydrophobic
                      and Hydrophilic Interactions / Indoles: chemistry / Indoles:
                      metabolism / Ligands / Microtubule-Associated Proteins:
                      chemistry / Microtubule-Associated Proteins: metabolism /
                      Models, Molecular / Molecular Sequence Data / Protein
                      Conformation / Receptors, GABA-A: metabolism / Substrate
                      Specificity / Titrimetry / Tryptophan: metabolism / Adaptor
                      Proteins, Signal Transducing (NLM Chemicals) / Indoles (NLM
                      Chemicals) / Ligands (NLM Chemicals) /
                      Microtubule-Associated Proteins (NLM Chemicals) / Receptors,
                      GABA-A (NLM Chemicals) / Tryptophan (NLM Chemicals) / J
                      (WoSType)},
      cin          = {INB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Chemistry, Medicinal},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18567048},
      UT           = {WOS:000258092300014},
      doi          = {10.1002/cbic.200800117},
      url          = {https://juser.fz-juelich.de/record/62893},
}