Strong and weak zinc binding sites in human zinc-alpha 2-glycoprotein

Aditya Kumar, Debolina Hati, Thana'a Mohajer Thaker, Layeque Miah, Philip Cunningham, Carmen Domene Nunez, Tam T. T. Bui, Alex F. Drake, Lindsay McDermott

Research output: Contribution to journalArticlepeer-review

16 Citations (SciVal)


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.
Original languageEnglish
Pages (from-to)3949-3954
Number of pages6
JournalFEBS Letters
Issue number24
Publication statusPublished - 11 Dec 2013


  • Zinc alpha 2 glycoprotein, Adipokine, ICP-MS, Spectroscopy, Molecular modeling, LIGAND-BINDING, MACULAR-DEGENERATION, BOUND ZINC, PROTEINS, ZN-ALPHA(2)-GLYCOPROTEIN, ZAG


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