| Literature DB >> 10570243 |
B B Kragelund1, J Knudsen, F M Poulsen.
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 alpha-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.Entities:
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Year: 1999 PMID: 10570243 DOI: 10.1016/s1388-1981(99)00151-1
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002