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Updated: May 6, 2026

Author Spotlight: Exploring Cellular Zinc Regulation Through ZnT1 Functionality
Published on: June 2, 2023
Strong and weak zinc binding sites in human zinc-α2-glycoprotein
Aditya Arun Kumar1, Debolina Hati, Thana'a Mohajer Thaker
1Department of Biochemistry, King's College London, Franklin Wilkins Building, 150 Stamford Street, London SE1 9NH, UK.
Abstract:
Zinc-α2-glycoprotein (ZAG) is an adipokine with an MHC class I-like protein fold. Even though zinc causes ZAG to precipitate from plasma during protein purification, no zinc binding has been identified to date. Using mass spectrometry, we demonstrated that ZAG contains one strongly bound zinc ion, predicted to lie close to the α1 and α2 helical groove. UV, CD and fluorescence spectroscopies detected weak zinc binding to holo-ZAG, which can bind up to 15 zinc ions. Zinc binding to 11-(dansylamino) undecanoic acid was enhanced by holo-ZAG. Zinc binding may be important for ZAG binding to fatty acids and the β-adrenergic receptor.
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