PHASING AND SOLVING THE CRYSTAL STRUCTURE OF A PORTION OF A STAU PROTEIN

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 Stau蛋白的一个区域已经结晶，我已经获得了高达1.5埃的自然衍射。我现在正试图使用I3C(5-氨基-2，4，6-三碘间苯二甲酸)或汞(乙基汞磷酸)的异常信号来获取相信息，它们已经被浸泡在晶体中。 获得这种蛋白质以前未知的结构对于理解Stau介导的衰退机制非常重要，这是我在Lynne Maquat的实验室研究的一个机制，我是博士后。当STAU与其同源RNA靶标结合时，这种机制以翻译依赖的方式有条件地降解mRNA，从而控制该特定蛋白在细胞中的丰度。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. A region of the STAU protein has been crystallized and I have obtained native diffraction up to 1.5 angstroms. I am now trying to obtain phase information using the anomolous signal of either I3C (5-amino-2,4,6-triiodoisophthalic acid), or Hg (ethyl mercuric phosphate), which have been soaked into the crystals. Obtaining the previously unkown structure of this protein is very important to understanding the mechanism of Stau mediated decay, which is a mechanim studied in Lynne Maquat`s lab where I am a postdoc. This mechanism conditionally degrades mRNA in a translationally dependent manner when STAU is bound to its cognate RNA target, thus controlling that particular protein`s abundance in the cell.