MCMV USP DOMAIN IN COMPLEX WITH AN UBIQUITIN-BASED SUICIDE SUBSTRATE

MCMV USP 结构域与基于泛素的自杀底物复合

• 批准号: 7721235
• 负责人: RACHELLE GAUDET
• 金额: $ 0.35万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-05-15 至 2009-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721235
• 关键词: Complex; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Herpesviridae; Herpesvirus 1; Homologous Gene; Human Herpesvirus 4; In Vitro; Institution; Murid herpesvirus 1; N-terminal; Proteins; Reaction; Research; Research Personnel; Resources; Source; Substrate Specificity; Ubiquitin; United States National Institutes of Health; base; insight; member; novel; suicide substrates; three dimensional structure

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 largest tegument protein of herpes simplex virus 1 (HSV-1), UL36, contains a novel deubiquitinating activity embedded in it. All members of the Herpesviridae contain a HSV-1 UL36homologue, the N-terminal segment of which show perfect conservation of putative catalytic residues. Homologs from HSV-1, murine cytomegalovirus (MCMV) and Epstein-Barr virus (EBV), chosen as representatives of the beta- and gammaherpesvirus subfamilies, respectively, were shown to display a deubiquitinating activity in vitro as well. The conservation of this activity throughout all subfamilies is indicative of an important, if not essential, function. In order to gain insights into substrate specificity and the reaction mechanism of the deubiquitinating activity of Herpesviridae, we aim to determine three-dimensional structures of N-terminal segments of HSV-1 UL36 and homologous segments of MCMV and EBV featuring this novel deubiquitinating activity.

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， 因此可以在其他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。 单纯疱疹病毒1型（HSV-1）最大的被膜蛋白UL 36具有去泛素化活性，所有疱疹病毒科成员都含有一个UL 36同源物，其N-末端具有保守的催化活性残基。来自HSV-1、鼠巨细胞病毒（MCMV）和EB病毒（EBV）的同源物（分别被选为β和γ疱疹病毒亚科的代表）也显示出体外去泛素化活性。这种活性在所有亚科中的保存表明了一种重要的（如果不是必需的）功能。为了深入了解疱疹病毒的底物特异性和去泛素化活性的反应机制，我们的目标是确定HSV-1 UL 36的N-末端片段和具有这种新的去泛素化活性的MCMV和EBV的同源片段的三维结构。