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Strong and weak zinc binding sites in human zinc-α2-glycoprotein

  • Lindsay McDermott
    ,
  • Aditya Arun Kumar
    ,
  • Debolina Hati
    ,
  • Thana'a Mohajer Thaker
    ,
  • Layeque Miah
    ,
  • Phil Cunningham
  • King's College London
    ,
  • University of Oxford
Research Output: Contribution to journal Article Peer-review

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.

Publication Information

Output type

Research Output: Contribution to journal Article Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 3949-54

Journal (Volume, Issue Number)

FEBS Letters (Volume 587, Issue 24)

Publication milestones

  • Published - 01/11/2013

Publication status

Published - 01/11/2013

ISSN

0014-5793

External Publication IDs

  • handle.net: 10547/622676
  • Scopus: 84888642160

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