Lortat-Jacob H, Grimaud J A
Unité de Pathologie Cellulaire, CNRS URA 602, Institut Pasteur, Lyon, France.
Cell Mol Biol. 1991;37(3):253-60.
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.
干扰素-γ C末端的结构与功能已得到广泛研究。位于该结构域的一个碱性氨基酸簇参与了蛋白质的三维结构构建，并且对其生物学活性至关重要。这一特定的氨基酸基团还参与干扰素-γ与基底膜或细胞表面硫酸乙酰肝素的结合。一旦与硫酸乙酰肝素结合，干扰素-γ就受到保护而不被蛋白水解切割，并且有人提出该蛋白质会折叠成一种新的松弛构象，稳定性有所增强。
