CRYSTAL STRUCTURE OF THE CED-9/CED-4/CED-3 TERNARY COMPLEX

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。细胞凋亡在后生动物的发育和动态平衡中起着至关重要的作用。线虫程序性细胞死亡(凋亡)的遗传学特征确定了CED-3、CED-4、CED-9和EGL-1四种蛋白质，它们共同控制着细胞凋亡的开始。CED-3是一种半胱氨酸氨基转移酶，其激活依赖于CED-4。CED-9拮抗CED-4的作用机制不明。CED-3、CED-4和CED-9形成杂低聚物。为了阐明线虫细胞死亡控制的机制，我们结晶了CED-3/CED-4/CED-9三元络合物。我们计划通过分子置换或MAD来确定结构。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Apoptosis plays an essential role in the development and homeostasis of metazoans. The genetic characterization of programmed cell death (apoptosis) in C. elegans identified four proteins, CED-3, CED-4, CED-9, and EGL-1, that collectively control the onset of apoptosis. CED-3 is a caspase and its activation depends on CED-4. CED-9 antagonize the function of CED-4 through an unknown mechanism. CED-3, CED-4, and CED-9 form a hetero-oligomer. To elucidate the mechanisms of cell death control in C. elegans, we crystallized the ternary complex of CED-3/CED-4/CED-9. We plan to determine the structure by molecular replacement or by MAD.