STRUCTURE DETERMINATION OF EUKARYOTIC TRANSCRIPTION FACTOR TAF1 ALPHA

这个子项目是许多研究子项目中的一个 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。 腺病毒（Ad）基因组与病毒核心蛋白（称为Ad core）复合，是早期基因转录和Ad感染细胞中第一轮复制的模板。一种称为模板激活因子-I（TAF-I）的细胞蛋白被发现参与体外Ad核心的重塑。我们发现TAF-I在感染的早期阶段通过感染细胞中的核心蛋白VII与Ad DNA相互作用。使用重组蛋白的体外结合试验表明，TAF-I与DNA蛋白VII复合物形成三元复合物。我们用悬滴法结晶了人TAF 1蛋白。晶体结构应该揭示病毒和宿主之间的蛋白质-蛋白质相互作用，并为药物设计提供一些想法。

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.