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

定相并解析 STAU 蛋白部分的晶体结构

• 批准号: 8363563
• 负责人: Lynne E Maquat
• 金额: $ 0.5万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-07-01 至 2012-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363563
• 关键词: Acids; Binding; Cells; Funding; Grant; Indole-3-Carbinol; Mediating; Messenger RNA; National Center for Research Resources; Phase; Postdoctoral Fellow; Principal Investigator; Proteins; RNA; Research; Research Infrastructure; Resources; Signal Transduction; Source; Structure; United States National Institutes of Health; cost; inorganic phosphate; protein structure

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.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 STAU 蛋白的一个区域已经结晶，我获得了高达 1.5 埃的天然衍射。 我现在尝试使用 I3C（5-氨基-2,4,6-三碘间苯二甲酸）或 Hg（磷酸乙基汞）的反常信号来获取相位信息，这些信号已浸入晶体中。 获得这种蛋白质以前未知的结构对于理解 Stau 介导的衰变机制非常重要，这是我在 Lynne Maquat 实验室研究的一种机制，我是该实验室的博士后。 当 STAU 与其同源 RNA 靶标结合时，这种机制会以翻译依赖性方式有条件地降解 mRNA，从而控制细胞中特定蛋白质的丰度。