STRUCTURE OF A BACTERIA TIR CONTAINING VIRULENCE FACTOR

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。 为了深入了解这一新的毒力因子家族的功能，确定TIR结构域在信号活性全长同源二聚体中的构象是至关重要的。我们希望SAXS数据给我们二聚体的方向：TIR结构域是与伙伴分子的TIR相反，还是N-末端螺旋区？在解决了TIR结构域的结构之后，我们的当务之急是找到一种快速的方法，因为它的功能相关性，可以提供二聚体组织的经验证据。

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. In order to get insights into the function of this new family of virulence factors it is crucial to ascertain the conformation of the TIR domain inside the signaling active full length homodimer. We expect SAXS data to give us the orientation of the dimer: is the TIR domain opposing the TIR of the partner molecule or the N-terminal helical region? Having solved the structure of the TIR domain, our top priority is to find a quick method that could provide empirical evidence of the dimer organization because of its functional relevance.