Name:
Publisher version
View Source
Access full-text PDFOpen Access
View Source
Check access options
Check access options
Authors
Kumar, Aditya ArunHati, Debolina
Thaker, Thana'a Mohajer
Miah, Layeque
Cunningham, Phil
Domene, Carmen
Bui, Tam T. T.
Drake, Alex F.
McDermott, Lindsay C.
Affiliation
King's College LondonIssue Date
2013-11-01
Metadata
Show full item recordAbstract
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.Citation
Kumar, Hati, Thaker, Miah, Cunningham, Domene, Bui, Drake, McDermott (2013) 'Strong and weak zinc binding sites in human zinc-α2-glycoprotein', FEBS Letters, 587 (24), pp.3949-54.Publisher
WileyJournal
FEBS LettersPubMed ID
24188824Type
ArticleLanguage
enISSN
0014-5793ae974a485f413a2113503eed53cd6c53
10.1016/j.febslet.2013.10.026