Human interleukin-3 contains a discontinuous zinc binding domain.
Article Details
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Smit V, van Veelen PA, Tjaden UR, van der Greef J, Haaijman JJ
Human interleukin-3 contains a discontinuous zinc binding domain.
Biochem Biophys Res Commun. 1992 Sep 16;187(2):859-66.
- PubMed ID
- 1530641 [ View in PubMed]
- Abstract
The primary structure of human interleukin-3 contains two amino acid consensus sequences at Glutamate 22- Histidine 26 and Histidine 95-Histidine 98, that are characteristic for zinc binding proteins. Therefore, the hypothesis was tested that human interleukin-3 binds zinc specifically by either one or both sequences. Protein dotblotting, followed by probing with radioactive zinc demonstrated specific zinc binding of interleukin-3. Metal specificity was confirmed by competition experiments with 12 other divalent- and trivalent metal ions. Protease treatment combined with plasma desorption mass spectrometry was used to localize the zinc binding domain. Specific zinc binding was restricted to a fragment composed of Threonine 11-Lysine 28 and Asparagine 80-Lysine 100. It was found to decrease by a factor of five when either of these two amino acid stretches was missing. It is concluded that human interleukin-3 is a zinc binding protein. Interleukin-3 zinc binding capacity is largely determined by both moieties of the protein that contain the consensus sequences. In addition we propose that the zinc binding of hIL-3 is involved in (de)phosphorylation of the hIL-3 receptor.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Zinc Interleukin-3 Protein Humans UnknownNot Available Details Zinc acetate Interleukin-3 Protein Humans UnknownNot Available Details Zinc chloride Interleukin-3 Protein Humans UnknownBinderDetails Zinc sulfate, unspecified form Interleukin-3 Protein Humans UnknownBinderDetails