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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS
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The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS

机译：使用SIRAS解析凝血因子XII的FnI-EGF样串联结构域

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摘要

fCoagulation factor XII (FXII) is a key protein in the intrinsic coagulation and kallikrein-kinin pathways. It has been found that negative surfaces and amyloids, such as A beta fibrils, can activate FXII. Additionally, it has been suggested that FXII simulates cells and that it plays an important role in thrombosis. To date, no structural data on FXII have been deposited, which makes it difficult to support any hypothesis on the mechanism of FXII function. The crystal structure of the FnI-EGF-like tandem domain of FXII presented here was solved using experimental phases. To determine the phases, a SIRAS approach was used with a native and a holmium chloride-soaked data set. The holmium cluster was coordinated by the C-terminal tails of two symmetry-related molecules. Another observation was that the FnI domain was much more ordered than the EGF-like domain owing to crystal packing. Furthermore, the structure shows the same domain orientation as the homologous FnI-EGF-like tandem domain of tPA. The plausibility of several proposed interactions of these domains of FXII is discussed. Based on this FXII FnI-EGF-like structure, it could be possible that FXII binding to amyloid and negatively charged surfaces is mediated via this part of FXII.
机译：f凝血因子XII（FXII）是内在凝血和激肽释放酶激肽途径中的关键蛋白。已经发现，负表面和淀粉样蛋白，例如Aβ原纤维，可以激活FXII。另外，已经建议FXII模拟细胞并且它在血栓形成中起重要作用。迄今为止，尚未存储有关FXII的结构数据，这使得很难支持有关FXII功能机制的任何假设。使用实验阶段解决了此处展示的FXII的FnI-EGF样串联结构域的晶体结构。为了确定相，将SIRAS方法与天然和氯化chloride浸泡的数据集一起使用。 two簇由两个对称相关分子的C末端尾部协调。另一观察结果是由于晶体堆积，FnI结构域比EGF样结构域更有序。此外，该结构显示出与tPA的同源FnI-EGF样串联结构域相同的结构域取向。讨论了FXII这些域的几种拟议的相互作用的合理性。基于这种FXII FnI-EGF样结构，FXII与淀粉样蛋白和带负电荷的表面的结合可能是通过FXII的这一部分介导的。

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