SOLUTION STRUCTURES DETERMINATION OF PROTEINS INVOLVED IN APOPTOSIS LE

程序性细胞死亡的起始事件 通过制备死亡结构域的可溶性复合物进行研究， 死亡效应域。 有限蛋白水解和质谱 对FADD、FLIP、FAS、RIP和TRADD进行了分析 蛋白质以限定功能结构域并构建合适的 过表达克隆以研究相互作用片段的结构 of these molecules分子. 上述蛋白质接收来自 肿瘤坏死因子受体（TNFR）的一个亚类，其含有 死亡领域。 第二类TNFR与TRAF分子相互作用 来传递一个信号，导致细胞增殖， 死亡 质谱和蛋白质印迹分析已应用于TRAF 2 定义最小交互作用域，定义交互作用 CD 30和CD 40表面，为全面结构分析做准备 TRAF/受体结构域复合物。

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.