7WQG

Bovin Alpha-lactalbumin binding with zinc ions

7WQG の概要

• エントリーDOI: 10.2210/pdb7wqg/pdb
• 分子名称: Alpha-lactalbumin, ZINC ION (3 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 84216.12

構造登録者

Li, T.,Zhang, T. (登録日: 2022-01-25, 公開日: 2022-08-31, 最終更新日: 2023-11-29)

主引用文献

Li, T.,Jiao, R.,Ma, J.,Zang, J.,Zhao, G.,Zhang, T.
Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells.
Rsc Adv, 12:21122-21128, 2022

PubMed Abstract: Zinc plays a vital role in structural, catalysis, and signal regulation in the human body. Zinc deficiency leads to the dysfunction of many organs and immunity systems. Diet proteins have distinct effects on zinc uptake. However, the mechanisms are uncovered. Here we select three principal components from whey protein: alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin, which bind with zinc at different affinities, to evaluate the relationship between their potential zinc uptake and protein binding. The experimental data shows that beta-lactoglobulin could promote zinc uptake, alpha-lactalbumin has minor effects, whereas bovine serum albumin reduced zinc uptake in Caco-2 cell lines. Zinc binding effects on protein structure were thoroughly inspected through fluorescent spectroscopy and X-ray crystallography. Isothermal titration calorimetry revealed that three proteins have different binding affinities toward zinc ions. We speculate that protein binding eliminates toxic effects from free zinc, and the binding strength dominates zinc uptake.

PubMed: 35975046
DOI: 10.1039/d2ra03565k

実験手法

X-RAY DIFFRACTION (2.5 Å)