Interferon-gamma C-terminal function: new working hypothesis. Heparan sulfate and heparin, new targets for IFN-gamma, protect, relax the cytokine and regulate its activity.
Structure and function of the interferon-gamma C-terminal extremity has been widely studied. A basic amino acid cluster located in this domain is involved in the tridimentional structure of the protein and is essential for the biological activity. This specific group of amino acid is also involved in the binding of interferon-gamma to basement membrane or cell surface heparan sulfate. Once bound to heparan sulfate, interferon-gamma is protected from proteolytic cleavage and it is suggested that the protein folds in a new relaxed conformation, with increased stability.
Unité de Pathologie Cellulaire, CNRS URA 602, Institut Pasteur, Lyon, France.
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H
Lortat-Jacob
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JA
Grimaud
D000595:Amino Acid Sequence; D006493:Heparin / Q000378:metabolism*; D006497:Heparan Sulfate / Q000378:metabolism; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship
D006493:Heparin; D006497:Heparan Sulfate; D007371:Interferon-gamma