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

doi:10.1016/j.febslet.2013.10.026

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

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

20 Citations (SciVal)

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.

Original language	English
Pages (from-to)	3949-3954
Number of pages	6
Journal	FEBS Letters
Volume	587
Issue number	24
DOIs	https://doi.org/10.1016/j.febslet.2013.10.026
Publication status	Published - 11 Dec 2013

Keywords

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

Access to Document

10.1016/j.febslet.2013.10.026

Cite this

@article{cf3014bf7fda446897a941e86454ce28,

title = "Strong and weak zinc binding sites in human zinc-alpha 2-glycoprotein",

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.",

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

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

year = "2013",

month = dec,

day = "11",

doi = "10.1016/j.febslet.2013.10.026",

language = "English",

volume = "587",

pages = "3949--3954",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "24",

}

TY - JOUR

T1 - Strong and weak zinc binding sites in human zinc-alpha 2-glycoprotein

AU - Kumar, Aditya

AU - Hati, Debolina

AU - Mohajer Thaker, Thana'a

AU - Miah, Layeque

AU - Cunningham, Philip

AU - Domene Nunez, Carmen

AU - Bui, Tam T. T.

AU - Drake, Alex F.

AU - McDermott, Lindsay

PY - 2013/12/11

Y1 - 2013/12/11

N2 - 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.

AB - 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.

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

UR - http://dx.doi.org/10.1016/j.febslet.2013.10.026

U2 - 10.1016/j.febslet.2013.10.026

DO - 10.1016/j.febslet.2013.10.026

M3 - Article

SN - 0014-5793

VL - 587

SP - 3949

EP - 3954

JO - FEBS Letters

JF - FEBS Letters

IS - 24

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this