| First Author | Kragelund BB | Year | 1999 |
| Journal | Biochim Biophys Acta | Volume | 1441 |
| Issue | 2-3 | Pages | 150-61 |
| PubMed ID | 10570243 | Mgi Jnum | J:58695 |
| Mgi Id | MGI:1349492 | Doi | 10.1016/s1388-1981(99)00151-1 |
| Citation | Kragelund BB, et al. (1999) Acyl-coenzyme A binding protein (ACBP). Biochim Biophys Acta 1441(2-3):150-61 |
| abstractText | 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. |
