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.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | B B A - Reviews on Cancer |
| Vol/bind | 1441 |
| Udgave nummer | 2-3 |
| Sider (fra-til) | 150-61 |
| Antal sider | 12 |
| ISSN | 0006-3002 |
| Status | Udgivet - 23 nov. 1999 |
Emneord
- Amino Acid Sequence
- Animals
- Carrier Proteins
- Diazepam Binding Inhibitor
- Humans
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Mutagenesis
- Sequence Alignment