• Author/Authors

    Birthe B. Kragelund، نويسنده , , Jens Knudsen، نويسنده , , Flemming M. Poulsen، نويسنده ,

  • DocumentNumber
    1601516
  • Title Of Article

    Acyl-coenzyme A binding protein (ACBP)

  • شماره ركورد
    11757
  • Latin Abstract
    Acyl-coenzyme A binding proteins are known from a large group of eukaryote species and to bind a long chain length acyl-CoA ester with very high affinity. Detailed biochemical mapping of ligand binding properties has been obtained as well as in-depth structural studies on the bovine apo-protein and of the complex with palmitoyl-CoA using NMR spectroscopy. In the four α-helix bundle structure, a set of 21 highly conserved residues present in more that 90% of all known sequences of acyl-coenzyme A binding proteins constitutes three separate mini-cores. These residues are predominantly located at the helix-helix interfaces. From studies of a large set of mutant proteins the role of the conserved residues has been related to structure, function, folding and stability.
  • From Page
    150
  • NaturalLanguageKeyword
    Two-state folding , Four-helix bundle , nuclear magnetic resonance
  • JournalTitle
    Studia Iranica
  • To Page
    161
  • To Page
    161