5LKF

Bovine beta-lactoglobulin complex with myristic acid at high pressure (0.55 GPa)

5LKF の概要

• エントリーDOI: 10.2210/pdb5lkf/pdb
• 関連するPDBエントリー: 5lke
• 分子名称: Beta-lactoglobulin, MYRISTIC ACID (3 entities in total)
• 機能のキーワード: beta-lactoglobulin, lipocalin, transport protein
• 由来する生物種: Bos taurus (Bovine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18529.54

構造登録者

Kurpiewska, K.,Lewinski, K.,Garbacz, K. (登録日: 2016-07-22, 公開日: 2016-08-17, 最終更新日: 2024-10-16)

主引用文献

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

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: 30174052
DOI: 10.1016/j.foodchem.2018.07.104

実験手法

X-RAY DIFFRACTION (2.5 Å)