CRYSTAL STRUCTURE OF VON WILLEBRAND FACTOR AL DOMAIN

我们希望利用同步辐射技术来确定 人血管性血友病因子（vWF）A1结构域的3D结构。 从该项目中获得的信息将有助于澄清 关键事件的机制和调控 止血，还参与病理性血栓形成。 目前认为天然vWF的结晶是不可能的， 由于大尺寸和异质性， 分子;因此这是获取3D信息的唯一方法 vWF的结构是集中在孤立的结构域。 结果 我们的研究预期将有助于定义vWF-GP Ib接触 研究中心，并将协助寻找vWF的特异性抑制剂 与抗血栓的重要靶点GP Ib结合 干预

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.