SOLUTION STRUCTURES DETERMINATION OF PROTEINS INVOLVED IN APOPTOSIS LE

程序性细胞死亡中的启动事件是 通过制备死亡结构域和可溶性络合物进行了研究 死亡效应域。限制性蛋白质降解和质谱学 对FADD、FLIP、Fas、RIP和TRADD进行了分析 蛋白质定义功能结构域并构建合适的 超量表达克隆研究相互作用片段的结构 这些分子中。上述蛋白质从 肿瘤坏死因子受体(TNFR)的一个子集，包含一个 死亡领地。第二类TNFR与TRAF分子相互作用 传递导致细胞增殖的信号，而不是细胞 死亡。对TRAF2进行了质谱学和蛋白质印迹分析 定义最小交互作用域，定义交互作用 CD30和CD40的表面，为全面结构分析做准备 TRAF/受体结构域复合体。

The initiation events in programmed cell death are being investigated by preparation of soluble complexes of death domains and death effector domains. Limited proteolysis and mass spectrometry analysis have been applied to the FADD, FLIP, FAS, RIP and TRADD proteins to define the functional domains and construct suitable overexpressing clones to study the structure of interacting segments of these molecules. The aforementioned proteins receive signals from a subset of tumor necrosis factor receptors (TNFRs) that contain a death domain. A second class of TNFRs interact with theTRAF molecules to transmit a signal that leads to cell proliferation instead of cell death. Mass spec and Western blot analysis have been applied to TRAF2 to define the minimal interacting domain, to define the interaction surface of CD30 and CD40 in preparation for a full structural analysis of a TRAF/receptor domain complex.