STRUCTURES OF CATALYTIC DOMAINS OF BLOOD PROTEINS

SEL2711(C40H58O6 Ng)是一个组合设计的活性中心 因子Xa抑制物(Ki=3 nm)和凝血酶抑制物(Ki=45M)。水晶 凝血酶-水杨酸的复合体已用于浸泡 凝血酶-水飞蓟素-SEL2711三元络合物的制备实验 晶体分析。计算出的电子密度图 X射线衍射数据表明没有两个C-末端 抑制剂的残留物。这是由于卵裂的结果 SEL2711和/或位于附近的残基无序 蛋白质的表面。因此，质谱学(MALDI-MS) 用于支持结晶学数据的精确独立 技术。络合物和SEL2711的质谱图表明 SEL2711被凝血酶切割，只去除一个C-末端 残留物。另一种残留物是从表面指出的 络合到液体分子间区，是无序的。

SEL2711 (C40H58O6Ng) is a combinatorially designed active site inhibitor of Factor Xa (Ki=3nM) and thrombin (Ki=45?M). The crystal of the complex of thrombin-hirugen has been used in a soaking experiment to obtain a ternary complex of thrombin-hirugen-SEL2711 for crystallographic analysis. The electron density map calculated from X-ray diffraction data indicates the absence of the two C-terminal residues of the inhibitor. This results from the cleavage of the SEL2711 and/or disorder of the residues which are located close to the surface of the protein. Therefore, the mass spectrometry (MALDI-MS) was used to support crystallographic data by a precise independent technique. Mass spectra of the complex and SEL2711 indicate that SEL2711 is cleaved by thrombin with the removal of only one C-terminal residue. The other residue is pointed out from the surface of the complex to the liquid intermolecular region and is disordered.