3UEV
Bovine beta-lactoglobulin complex with myristic acid
Summary for 3UEV
| Entry DOI | 10.2210/pdb3uev/pdb |
| Related | 3NPO 3NQ3 3NQ9 3QZJ 3QZK 3UEU 3UEW 3UEX |
| Descriptor | Beta-lactoglobulin, MYRISTIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta protein, beta-barrel, lipocalin, bovine milk, transport protein |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Secreted: P02754 |
| Total number of polymer chains | 1 |
| Total formula weight | 18621.64 |
| Authors | Loch, J.,Lewinski, K. (deposition date: 2011-10-31, release date: 2011-11-09, Last modification date: 2024-11-27) |
| Primary citation | Loch, J.I.,Polit, A.,Bonarek, P.,Olszewska, D.,Kurpiewska, K.,Dziedzicka-Wasylewska, M.,Lewinski, K. Bovine beta-lactoglobulin complex with myristic acid Int.J.Biol.Macromol., 50:1095-1102, 2012 Cited by PubMed Abstract: Lactoglobulin is a globular milk protein for which physiological function has not been clarified. Due to its binding properties lactoglobulin might serve as a carrier for bioactive molecules. Binding of 12-, 14-, 16- and 18-carbon saturated fatty acids to bovine β-lactoglobulin has been characterised by isothermal titration calorimetry and X-ray crystallography as a part of systematic studies of lactoglobulin complexes with ligands of biological importance. The thermodynamic parameters have been determined for lauric, myristic and palmitic acid complexes revealing systematic decrease of enthalpic and increase of entropic component of ΔG with elongation of aliphatic chain. In all crystal structures determined with resolution 1.9-2.1Å, single fatty acid molecule was found in the β-barrel in extended conformation with individual pattern of interactions. Location of a fatty acid in the binding site depends on the length of aliphatic chain and influences polar interactions between protein and ligand. Systematic changes of entropic component indicate important role of water in binding process. PubMed: 22425630DOI: 10.1016/j.ijbiomac.2012.03.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
