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@ARTICLE{Thielmann:7139,
      author       = {Thielmann, Y. and Weiergräber, O.H. and Mohrlüder, J. and
                      Willbold, D.},
      title        = {{S}tructural characterization of {GABARAP}-ligand
                      interactions},
      journal      = {Molecular BioSystems},
      volume       = {5},
      issn         = {1742-206X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry},
      reportid     = {PreJuSER-7139},
      pages        = {575 - 579},
      year         = {2009},
      note         = {O.H.W. is grateful to Georg Buldt for continuous generous
                      support. Moreover, assistance by the beamline staff at ESRF
                      (Grenoble, France) is acknowledged. This study was supported
                      by a research grant from the Deutsche Forschungsgemeinschaft
                      to D. W. (Wi1472/5).},
      abstract     = {The GABA(A) receptor-associated protein (GABARAP) plays an
                      important role in intracellular trafficking of several
                      proteins. It undergoes a C-terminal lipidation process that
                      enables anchoring in the cytosolic leaflet of cellular
                      membranes. While the three-dimensional structure of GABARAP
                      itself has been determined, structural investigation of
                      complexes with its interaction partners has just commenced.
                      Studies with indole derivatives revealed that GABARAP
                      features two hydrophobic binding sites (hp1 and hp2). These
                      also play an essential role in complex formation with the
                      native ligand calreticulin. Furthermore, a model of
                      hexameric N-ethylmaleimide-sensitive factor (NSF) suggests
                      that binding of GABARAP to this molecular machine may
                      involve a similar site. Since hp1 and hp2 are highly
                      conserved throughout the GABARAP family, the relevance of
                      the structural data presented here is likely to extend to
                      GABARAP homologues.},
      keywords     = {Amino Acid Sequence / Animals / Calreticulin: chemistry /
                      Calreticulin: metabolism / Clathrin Heavy Chains: chemistry
                      / Clathrin Heavy Chains: metabolism / Humans / Ligands /
                      Models, Molecular / Protein Binding / Protein Structure,
                      Tertiary / Receptors, GABA-A: chemistry / Receptors, GABA-A:
                      metabolism / Calreticulin (NLM Chemicals) / Ligands (NLM
                      Chemicals) / Receptors, GABA-A (NLM Chemicals) / Clathrin
                      Heavy Chains (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 / Programm
                      Biosoft},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19462014},
      UT           = {WOS:000266269500002},
      doi          = {10.1039/b900425d},
      url          = {https://juser.fz-juelich.de/record/7139},
}