Strong and weak zinc binding sites in human zinc-α2-glycoprotein
| Autor: | Debolina Hati, Aditya Arun Kumar, Layeque Miah, Alex F. Drake, Tam T. T. Bui, Phil Cunningham, Lindsay C. McDermott, Carmen Domene, Thana'a Mohajer Thaker |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Molecular model Biophysics chemistry.chemical_element Molecular modeling Zinc Mass spectrometry Biochemistry Protein Structure Secondary Substrate Specificity Zinc α2 glycoprotein Adipokines Structural Biology Adipokine Receptors Adrenergic beta Protein purification MHC class I Genetics Humans ICP-MS Protein Interaction Domains and Motifs Receptor Molecular Biology Spectroscopy Glycoproteins Binding Sites biology Chemistry Zinc-Alpha-2-Glycoprotein Fatty Acids Cell Biology Fluorescence Crystallography biology.protein Carrier Proteins Protein Binding |
| Zdroj: | FEBS letters. 587(24) |
| ISSN: | 1873-3468 0014-5793 |
| Popis: | 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. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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