• Title of article

    Ligand Binding Mode of GABAA Receptor-Associated Protein

  • Author/Authors

    Oliver H. Weiergr?ber، نويسنده , , Thomas Stangler، نويسنده , , Yvonne Thielmann، نويسنده , , Jeannine Mohrlüder، نويسنده , , Katja Wiesehan، نويسنده , , Dieter Willbold، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2008
  • Pages
    12
  • From page
    1320
  • To page
    1331
  • Abstract
    The γ-aminobutyric acid type A (GABAA) 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 GABAA receptor-associated protein complexed with a high-affinity synthetic peptide at 1.3 Å resolution. The data shed light on the probable binding modes of key interaction partners, including the GABAA 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
    GABARAP , GABAA receptor , phage display , synthetic peptide , X-ray crystallography
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2008
  • Journal title
    Journal of Molecular Biology
  • Record number

    1257368