THE IFS-SPN INTERFACE

这个子项目是许多利用 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。 位于圣路易斯的华盛顿大学的Caparon和Hultgren的研究小组最近发现了由化脓性链球菌分泌的蛋白质毒素（SPN，约36 kDa），化脓性链球菌是一种革兰氏阳性细菌，可引起链球菌性咽喉炎和食肉疾病。 最近发现一种新的内源性抑制因子，命名为SPN免疫因子（Immunity Factor for SPN，IFS，~ 22 kDa）。 IFS与SPN以1：1的摩尔比形成稳定的复合物，并通过充当竞争性抑制剂来抑制SPN的活性。 IFS的晶体结构由圣路易斯华盛顿大学的Ellenberger小组确定（未发表的数据）。 我们的目标是使用高分辨率的PLIMSTEX协议来定位IFS到SPN的绑定接口。 复杂的晶体结构正在进行中。

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. The teams of Caparon and Hultgren at Washington University in St. Louis recently identified the protein toxin (SPN, ~36 kDa) secreted by Streptococcus pyogenes, a Gram-positive bacteria responsible for causing strep throat and flesh eating disease. A novel endogenous inhibitor, named Immunity Factor for SPN (IFS, ~ 22kDa) was recently discovered on the same codon as SPN. IFS forms a stable complex with SPN at a 1:1 molar ratio and inhibits SPN's activity by acting as a competitive inhibitor. The crystal structure of IFS was determined in the Ellenberger group at Washington University in St. Louis (unpublished data). Our goal is to use the high resolution PLIMSTEX protocol to locate the binding interface of IFS to SPN. The crystal structure of the complex is underway.