TRYPANOSOMAL PHOSPHOGLYCERATE KINASE TRANSITION STATE & STRUC BASED DRUG DESIGN

锥虫磷酸甘油激酶过渡态

• 批准号: 6586736
• 负责人: BRADLEY BERNSTEIN
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586736
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; parasitism; proteins; radiography; structural biology; bioimaging /biomedical imaging; biomaterials; biomedical resource; parasitism; proteins; radiography; structural biology

We wish to use synchrotron radiation techniques to determine the 3D structure of the A1 domain of human von Willebrand factor (vWF). The information gained from this project will help clarify the mechanisms and regulation of a key event essential for normal hemostasis and also involved in pathological thrombosis. Crystallization of native vWF is considered impossible with currently available techniques due to the large size and heterogeneous nature of the molecule; thus the only approach to gain information on the 3D structure of vWF is to focus on isolated domains. The results expected from our studies will help in defining the vWF-GP Ib contact sites and will assist in searching for specific inhibitors of vWF binding to GP Ib, an important target for anti-thrombotic intervention.

我们希望使用同步加速器辐射技术来确定 人类von Willebrand因子（VWF）的A1域的3D结构。 从该项目中获得的信息将有助于澄清 正常必不可少的关键事件的机制和调节 止血，还参与病理血栓形成。 当前认为本机VWF的结晶被认为是不可能的 由于尺寸较大和异质性的可用技术 分子；因此，获取3D信息的唯一方法 VWF的结构是关注孤立的域。 结果 从我们的研究中预期将有助于定义VWF-GP IB联系 站点并将帮助搜索VWF的特定抑制剂 与GP IB结合，这是抗血栓形成的重要目标 干涉。