% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Weiergrber:344,
      author       = {Weiergräber, O. H. and Stangler, T. and Thielmann, Y. and
                      Mohrlüder, J. and Wiesehan, K. and Willbold, D.},
      title        = {{L}igand binding mode of {GABA}({A}) receptor-associated
                      protein},
      journal      = {Journal of molecular biology},
      volume       = {381},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-344},
      pages        = {1320 - 1331},
      year         = {2008},
      note         = {The authors wish to thank Joachim Granzin for helpful
                      discussion and Olga Dietz for excellent technical
                      assistance. O.H.W. is grateful to Georg Buldt for continuous
                      generous support. Moreover, assistance by the ESRF staff at
                      beamline ID14-1 is acknowledged. This study was supported by
                      a research grant from the Deutsche Forschungsgemeinschaft to
                      D.W. (Wi1472/5).},
      abstract     = {The gamma-aminobutyric acid type A (GABA(A))
                      receptor-associated protein is a versatile adaptor protein
                      playing an important role in intracellular vesicle
                      trafficking, particularly in neuronal cells. We present the
                      X-ray structure of the soluble form of human GABA(A)
                      receptor-associated protein complexed with a high-affinity
                      synthetic peptide at 1.3 A resolution. The data shed light
                      on the probable binding modes of key interaction partners,
                      including the GABA(A) receptor and the cysteine protease
                      Atg4. The resulting models provide a structural background
                      for further investigation of the unique biological
                      properties of this protein.},
      keywords     = {Adaptor Proteins, Signal Transducing: chemistry / Adaptor
                      Proteins, Signal Transducing: metabolism / Humans / Kinetics
                      / Ligands / Magnetic Resonance Spectroscopy /
                      Microtubule-Associated Proteins: chemistry /
                      Microtubule-Associated Proteins: metabolism / Models,
                      Molecular / Peptides: metabolism / Protein Binding / Protein
                      Structure, Secondary / Surface Plasmon Resonance / Adaptor
                      Proteins, Signal Transducing (NLM Chemicals) / GABARAP
                      protein, human (NLM Chemicals) / Ligands (NLM Chemicals) /
                      Microtubule-Associated Proteins (NLM Chemicals) / Peptides
                      (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18638487},
      UT           = {WOS:000259169100019},
      doi          = {10.1016/j.jmb.2008.06.086},
      url          = {https://juser.fz-juelich.de/record/344},
}