7WQL

Bovin Beta-lactoglobulin binding with zinc ions

Summary for 7WQL

• Entry DOI: 10.2210/pdb7wql/pdb
• Descriptor: Beta-lactoglobulin, ZINC ION (3 entities in total)
• Functional Keywords: metal binding protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 2
• Total formula weight: 36994.80

Authors

Li, T.,Ma, J.,Zang, J.,Zhao, G.,Zhang, T. (deposition date: 2022-01-25, release date: 2022-08-31, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.001 Å)