Kinoshita Takayoshi, Nakanishi Isao, Sato Akihiro, Tada Toshiji
Exploratory Research Laboratories, Fujisawa Pharmaceutical Co. Ltd., 5-2-3, Tokodai, Tsukuba, Ibaraki 300-2698, Japan.
Bioorg Med Chem Lett. 2003 Jan 6;13(1):21-4. doi: 10.1016/s0960-894x(02)00852-1.
The crystal structure of porcine pancreatic elastase (PPE) complexed with a potent peptidyl inhibitor, FR136706, was solved at 2.2A resolution. FR136706 fits snugly into the extended active site pocket. The benzene moiety of FR136706 induced dramatic movement of the side chain moiety of Arg217 and both moieties formed a pi-pi interaction, which has never been found previously in structures of PPE complexed with inhibitors. This novel interaction mode may lead to design of new types of inhibitors.
猪胰弹性蛋白酶（PPE）与强效肽基抑制剂FR136706形成的复合物的晶体结构在2.2埃分辨率下得到解析。FR136706紧密地契合在延伸的活性位点口袋中。FR136706的苯环部分诱导了Arg217侧链部分的显著移动，并且这两个部分形成了π-π相互作用，这种相互作用在之前PPE与抑制剂形成的复合物结构中从未被发现过。这种新型的相互作用模式可能会引领新型抑制剂的设计。
