5LKF
Bovine beta-lactoglobulin complex with myristic acid at high pressure (0.55 GPa)
Summary for 5LKF
| Entry DOI | 10.2210/pdb5lkf/pdb |
| Related | 5lke |
| Descriptor | Beta-lactoglobulin, MYRISTIC ACID (3 entities in total) |
| Functional Keywords | beta-lactoglobulin, lipocalin, transport protein |
| Biological source | Bos taurus (Bovine) |
| Total number of polymer chains | 1 |
| Total formula weight | 18529.54 |
| Authors | Kurpiewska, K.,Lewinski, K.,Garbacz, K. (deposition date: 2016-07-22, release date: 2016-08-17, Last modification date: 2024-10-16) |
| Primary citation | Kurpiewska, K.,Biela, A.,Loch, J.I.,Lipowska, J.,Siuda, M.,Lewinski, K. Towards understanding the effect of high pressure on food protein allergenicity: beta-lactoglobulin structural studies. Food Chem, 270:315-321, 2019 Cited by PubMed Abstract: A number of studies were devoted to understanding an immunological effect of pressure-treated β-lactoglobulin. In our previous work we have proved that high pressure significantly modifies β-lactoglobulin conformation and consequently its physicochemical properties. Here, structure of β-lactoglobulin complex with myristic acid determined at the highest accepted by the crystal pressure value of 550 MPa is reported. Our results structurally prove that pressure noticeably modifies positions of the major β-lactoglobulin epitopes. Considering the biological impact of observed changes in epitope regions, high pressure β-lactoglobulin structure presents a step forward in understanding the pressure modification of food protein allergenicity. The conformational changes of pressurized β-lactoglobulin did not support the hypothesis that proteolytic digestion facilitated by pressure is caused by an exposure of the digestive sites. Our findings demonstrate that high pressure protein crystallography can potentially identify the most pressure-sensitive fragments in allergens, and can therefore support development of hypoallergenic food products. PubMed: 30174052DOI: 10.1016/j.foodchem.2018.07.104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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