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的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 细胞凋亡抑制因子（Inhibitors of apoptosis，IAP）是一种多结构域的抗凋亡因子，可阻断细胞死亡。IAP家族成员含有具有E3泛素连接酶活性的C-末端RING结构域。小分子拮抗剂与细胞IAP（cIAP）内的IAP重复的结合促进cIAP自动泛素化和蛋白酶体降解，从而释放cIAP对细胞凋亡的抑制。远离RING结构域的小分子结合诱导连接酶活性，以及我们想要理解的构象变化。我们寻求小分子拮抗剂存在和不存在下的cIAP 1的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.