Conformation of a bound inhibitor of blood coagulant factor Xa.
Conformation of a bound inhibitor of blood coagulant factor Xa.
复制标题
凝血因子 Xa 的结合抑制剂的构象。
DOI：
10.1021/bi027369g
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发表时间：
2003
期刊：
影响因子：
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通讯作者：
Schaefer,Jacob
中科院分区：
文献类型：
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作者：
Studelska,DanielR;McDowell,LyndaM;Adler,Marc;O'Connor,RobertD;Mehta,AnilK;Guilford,WilliamJ;Dallas,JerryL;Arnaiz,Damian;Light,DavidR;Schaefer,Jacob
13 C {15 N}和13 C {19 F}旋转回波双共振NMR已被用于表征ZK-816042的酶结合结构，ZK-816042是一种人因子Xa（FXa）的脒-咪唑啉抑制剂。NMR实验在冻干的FXa−抑制剂复合物上进行。在稳定赋形剂的存在下在溶液中形成复合物，并在冻干前逐渐过冷后冷冻。结果表明，缓蚀剂与咪唑啉环的取向分布结合。
13C{15N} and13C{19F} rotational-echo double-resonance NMR have been used to characterize the enzyme-bound structure of ZK-816042, an amidine−imidazoline inhibitor of human factor Xa (FXa). The NMR experiments were performed on a lyophilized FXa−inhibitor complex. The complex was formed in solution in the presence of stabilizing excipients and frozen after gradual supercooling prior to lyophilization. The results indicate that the inhibitor binds with a distribution of orientations of the imidazoline ring.