DETERMINATION OF THE STRUCTURE OF VITAMIN K EPOXIDE REDUCTASE (VKOR)

维生素 K 环氧还原酶 (VKOR) 结构的测定

• 批准号: 7955145
• 负责人: Tom A Rapoport
• 金额: $ 2.14万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-04-01 至 2010-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955145
• 关键词: Bacteria; Blood Coagulation Factor; Blood coagulation; Computer Retrieval of Information on Scientific Projects Database; Disulfides; Funding; Goals; Grant; Homologous Gene; Hydroquinones; Institution; Light; Proteins; Research; Research Personnel; Resources; Roentgen Rays; Source; Structure; United States National Institutes of Health; Vitamin K; Warfarin; carboxylate; cofactor; hydroquinone; inhibitor/antagonist; reduced vitamin K; structural biology; vitamin K epoxide reductase; vitamin K1 oxide

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. VKOR reduces vitamin K epoxide to the hydroquinone form of vitamin K. Reduced vitamin K is a cofactor for a carboxylase that gamme-carboxylates several proteins, including several blood coagulation factors. VKOR is the target for warfarin, the major blood coagulation inhibitor. Homologs of VKOR exist in several bacteria and have recently been shown to be involved in disulfide bridge formation. The goal of this project is to determine an Xray structure of one of these homologs. The structure would likely shed light on the mechanism of disulfide bridge formation and warfarin inhibition.

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。 VKOR将维生素K环氧化物还原为维生素K的氢醌形式。 还原型维生素K是羧化酶的辅因子，羧化酶使几种蛋白质（包括几种凝血因子）γ-羧化。VKOR是华法林（主要凝血抑制剂）的靶点。VKOR的同源物存在于几种细菌中，最近已被证明参与二硫键的形成。该项目的目标是确定这些同系物之一的X射线结构。该结构可能有助于阐明二硫键形成和华法林抑制的机制。