NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides.

ABSTRACT: Interferons are cytokines that play a complex role in the resistance of mammalian hosts to pathogens. IFNgamma (interferon-gamma) is secreted by activated T-cells and natural killer cells. IFNgamma is involved in a wide range of physiological processes, including antiviral activity, immune response, cell proliferation and apoptosis, as well as the stimulation and repression of a variety of genes. IFNgamma activity is modulated by the binding of its C-terminal domain to HS (heparan sulphate), a glycosaminoglycan found in the extracellular matrix and at the cell surface. In the present study, we analysed the interaction of isolated heparin-derived oligosaccharides with the C-terminal peptide of IFNgamma by NMR, in aqueous solution. We observed marked changes in the chemical shifts of both pe

SUBMITTER: Vanhaverbeke C 

PROVIDER: S-EPMC1134092 | biostudies-literature | 2004 Nov

REPOSITORIES: biostudies-literature