STRUCTURAL STUDIES OF AN ADENINE DNA GLYCOSYLASE, MUTY

腺嘌呤 DNA 糖基化酶 MUTY 的结构研究

• 批准号: 8169328
• 负责人: GREGORY Lawrence VERDINE
• 金额: $ 0.35万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169328
• 关键词: 2' -deoxyadenosine; Adenine; Binding; Catalysis; Computer Retrieval of Information on Scientific Projects Database; DNA; DNA glycosylase; Funding; Grant; Institution; Light; Research; Research Personnel; Resources; Roentgen Rays; Source; Structure; United States National Institutes of Health; enzyme mechanism; inhibitor/antagonist; insight; mutY adenine glycosylase; nucleobase; programs

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. MutY is an adenine DNA glycosylase that recognizes adenine nucleobase opposite 8-oxoguanine and catalyzes the cleavage of the N-glycosidic bond of the substrate 2'-deoxyadenosine. Although the previous X-ray crystallographic study provided significant insights into 8-oxoguanine recognition by MutY, the substrate adenine recognition and catalysis mechanisms by this enzyme are poorly understood, due in significant part to use of an enzymatically inactive MutY. Our program aims to shed light into these mechanisms by determining an X-ray structure of a catalytically active MutY bound to its inhibitor DNA.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 Muty是一种腺嘌呤DNA糖基化酶，它识别腺嘌呤核苷酸酶相对于8-氧气，并催化底物2'-脱氧腺苷的N-糖苷键的裂解。 尽管先前的X射线晶体学研究通过MUTY对8-氧气素识别提供了重大见解，但该酶的底物腺嘌呤识别和催化机制的理解很少，这在很大程度上是由于使用了酶促的无效muty。我们的计划旨在通过确定与其抑制剂DNA结合的催化活性muty的X射线结构来阐明这些机制。