CIAP CONFORMATIONAL CHANGE AND OLIGOMERIZATION CAUSED BY A SMALL MOLECULE ANTAGO

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 细胞凋亡抑制因子(IAPs)是一类多结构域的抗细胞凋亡因子，可阻断细胞死亡。IAP家族成员含有一个具有E3泛素连接酶活性的C-末端环区。小分子拮抗剂与细胞内IAP重复序列(CIAP)结合可促进CIAP自身泛素化和蛋白酶体降解，从而释放CIAP对细胞凋亡的抑制作用。远离环状结构域的小分子结合诱导连接酶活性，以及我们想要了解的构象变化。我们从没有和存在小分子拮抗剂的情况下从cIAP1获得SAXS数据。

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. Inhibitors of apoptosis (IAPs) are multi-domain anti-apoptotic factors that can block cell death. IAP family members contain a C-terminal RING domain with E3 ubiquitin ligase activity. Binding of small molecule antagonists to IAP repeats within cellular IAPs (cIAPs) promotes cIAP auto- ubiquitination and proteasomal degradation, thereby releasing cIAP inhibition of apoptosis. Small molecule binding remote from the RING domain induces ligase activity, and a conformational change we want to understand. We seek SAXS data from cIAP1 both in the absence and presence of small molecule antagonists.