STRUCTURES OF CATALYTIC DOMAINS OF BLOOD PROTEINS

SEL 2711（C40 H58 O 6 Ng）是一个组合设计的活性位点 Xa因子抑制剂（Ki= 3 nM）和凝血酶抑制剂（Ki=45？M）。 晶体 凝血酶-水蛭素复合物已用于浸泡 实验以获得凝血酶-水蛭素-SEL 2711的三元复合物， 晶体学分析 电子密度图由 X-射线衍射数据表明不存在两个C-末端 抑制剂的残留物。 这是由于分裂的 SEL 2711和/或位于靠近SEL 2711的残基的紊乱。 蛋白质的表面。 因此，质谱（MALDI-MS） 被用来支持晶体学数据， 法 络合物和SEL 2711的质谱表明， SEL 2711被凝血酶切割，仅去除一个C-末端 残余物 另一个残留物是从表面上指出的， 复合物的液体分子间区域和无序。

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.