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

被引：23
|
作者：
Kumar, Aditya Arun [1 ]
Hati, Debolina [1 ]
Thaker, Thana'a Mohajer [1 ]
Miah, Layeque [1 ]
Cunningham, Phil [1 ]
Domene, Carmen [2 ,4 ]
Bui, Tam T. T. [5 ]
Drake, Alex F. [5 ]
McDermott, Lindsay C. [3 ]
机构：
[1] Kings Coll London, Dept Biochem, London SE1 9NH, England
[2] Kings Coll London, Dept Chem, London SE1 9NH, England
[3] Kings Coll London, Diabet & Nutr Sci Div, London SE1 9NH, England
[4] Univ Oxford, Chem Res Lab, Oxford OX1 3TA, England
[5] Kings Coll London, Biomol Spect Ctr, Opt & Chiropt Spect Facil, London SE1 1UL, England
来源：
FEBS LETTERS | 2013年 / 587卷 / 24期
关键词：
Zinc alpha 2 glycoprotein; Adipokine; ICP-MS; Spectroscopy; Molecular modeling; LIGAND-BINDING; BOUND ZINC; ZN-ALPHA(2)-GLYCOPROTEIN; ZAG;
D O I：
10.1016/j.febslet.2013.10.026
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Zinc-alpha 2-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 alpha 1 and alpha 2 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 beta-adrenergic receptor. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：3949 / 3954
页数：6
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