STRUCTURE DETERMINATION OF EUKARYOTIC TRANSCRIPTION FACTOR TAF1 ALPHA

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。 腺病毒(Ad)基因组与病毒核心蛋白形成复合体，称为Ad core，是早期基因转录的模板，也是Ad感染细胞进行第一轮复制的模板。一种被命名为模板激活因子-I(TAF-I)的细胞蛋白被发现在体外参与了Ad core的重塑。我们发现在感染的早期，TAF-I通过感染细胞中的核心蛋白VII与Ad DNA相互作用。重组蛋白的体外结合分析表明，TAF-I与DNA蛋白VII形成三元复合体。我们用悬滴法对人TAF1蛋白进行了结晶。晶体结构将有助于揭示病毒与宿主之间的蛋白质相互作用，并为药物设计提供一些思路。

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 adenovirus (Ad) genome complexed with viral core proteins designated Ad core is the template for transcription of early genes and the first round of replication in Ad-infected cells. A cellular protein designated template-activating factor-I (TAF-I) is found to be involved in remodeling of the Ad core in vitro. We found that TAF-I interacts with the Ad DNA through core protein VII in infected cells in early phases of infection. In vitro binding assays using recombinant proteins showed that TAF-I forms ternary complexes with DNA¿¿¿¿¿protein VII complexes. We crystallized the human TAF1 protein by the hanging-drop method. The crystal structure should shed light on the protein-protein interaction between virus and host, and give some idea of the drug design.