True interaction mode of porcine pancreatic elastase with FR136706, a potent peptidyl inhibitor
True interaction mode of porcine pancreatic elastase with FR136706, a potent peptidyl inhibitor
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DOI：
10.1016/s0960-894x(02)00852-1
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发表时间：
2003-01-06
影响因子：
2.7
通讯作者：
Tada, T
中科院分区：
文献类型：
--
作者：
Kinoshita, T;Nakanishi, I;Tada, T
以2.2埃分辨率解析了猪胰弹性蛋白酶（PPE）与肽基抑制剂FR 136706复合物的晶体结构。FR 136706紧密贴合在延长的活性部位囊袋中。FR 136706的苯部分诱导Arg 217的侧链部分的剧烈移动，并且两个部分形成pi-pi相互作用，这在先前与抑制剂复合的PPE结构中从未发现。这种新的相互作用模式可能会导致设计新类型的抑制剂。(C)2002爱思唯尔科技有限公司版权所有。
The crystal structure of porcine pancreatic elastase (PPE) complexed with a potent peptidyl inhibitor FR136706, was solved at 2.2Angstrom 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. (C) 2002 Elsevier Science Ltd. All rights reserved.