Szente B E, Johnson H M
Department of Microbiology, University of Florida, Gainesville 32611.
Biochem Biophys Res Commun. 1994 May 30;201(1):215-21. doi: 10.1006/bbrc.1994.1691.
We have previously shown that murine interferon gamma (IFN gamma) binds to a soluble form of its receptor via both the N-terminus and C-terminus. The IFN gamma N-terminus binds extracellular receptor residues 95-120. Here we report that the C-terminus of IFN gamma binds to the membrane proximal region of the cytoplasmic domain of the receptor, residues 253-287. Peptide binding to fixed/permeabilized cells is specifically blocked by anti-(253-287) antibodies. These data suggest a novel mechanism by which IFN gamma binds to its receptor, involving both the extracellular and the intracellular receptor domains. Such a mechanism could have broader implications for the activation of signal transduction pathways by both IFN gamma and other cytokines whose receptors are members of the cytokine receptor superfamily.
我们之前已经表明，小鼠干扰素γ（IFNγ）通过N端和C端与可溶性形式的受体结合。IFNγ的N端与细胞外受体残基95 - 120结合。在此我们报告，IFNγ的C端与受体细胞质结构域的膜近端区域结合，即残基253 - 287。抗（253 - 287）抗体可特异性阻断肽与固定/通透细胞的结合。这些数据提示了一种IFNγ与其受体结合的新机制，涉及细胞外和细胞内受体结构域。这种机制可能对IFNγ以及其他受体属于细胞因子受体超家族的细胞因子激活信号转导途径具有更广泛的意义。
