Matsuzaki T, Sasaki C, Okumura C, Umeyama H
Research Center, Mitsubishi Chemical Industries Ltd., Kanagawa.
J Biochem. 1989 Jun;105(6):949-52. doi: 10.1093/oxfordjournals.jbchem.a122785.
The three-dimensional structure of a thrombin inhibitor-trypsin complex has been determined by an X-ray analysis at 2.5 A resolution. The result has given experimental support to the mechanisms previously proposed by the authors for the selective inhibition of trypsin, thrombin, factor Xa, and plasmin by inhibitors with an arginine or lysine backbone. The differences in the amino acid sequences at the positions corresponding to Ilc63, Leu99, and Ser190 of trypsin give each enzyme different binding affinities toward inhibitors and result in the selective inhibition. Furthermore, the X-ray analysis has revealed a novel type of interaction between the inhibitor and trypsin. The hydrogen bonds between the inhibitor main chain and trypsin Gly216 play an essential role in the complex formation.
已通过分辨率为2.5埃的X射线分析确定了凝血酶抑制剂 - 胰蛋白酶复合物的三维结构。该结果为作者先前提出的关于具有精氨酸或赖氨酸主链的抑制剂对胰蛋白酶、凝血酶、因子Xa和纤溶酶进行选择性抑制的机制提供了实验支持。胰蛋白酶中与Ile63、Leu99和Ser190相对应位置的氨基酸序列差异，使每种酶对抑制剂具有不同的结合亲和力，从而导致选择性抑制。此外，X射线分析揭示了抑制剂与胰蛋白酶之间一种新型的相互作用。抑制剂主链与胰蛋白酶Gly216之间的氢键在复合物形成中起关键作用。
