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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
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High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.

机译：高分辨率的三个新结构trypsin-squash-inhibitor复合物:详细与其他胰蛋白酶和他们比较复合物。

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摘要

An anionic trypsin from Atlantic salmon and bovine trypsin have been complexed with the squash-seed inhibitors, CMTI-I (Cucurbita maxima trypsin inhibitor I, P1 Arg) and CPTI-II (Cucurbita pepo trypsin inhibitor II, P1 Lys). The crystal structures of three such complexes have been determined to 1.5-1.8 A resolution and refined to crystallographic R factors ranging from 17.6 to 19.3%. The two anionic salmon-trypsin complexes (ST-CPTI and ST-CMTI) and the bovine-trypsin complex (BT-CPTI) have been compared to other trypsin-inhibitor complexes by means of general structure and primary and secondary binding features. In all three new structures, the primary binding residue of the inhibitor binds to trypsin in the classical manner, but with small differences in the primary and secondary binding patterns. Lysine in CPTI-II binds deeper in the specificity pocket of bovine trypsin than lysine in other known lysine-bovine-trypsin complexes, and anionic salmon trypsin lacks some of the secondary binding interactions found in the complexes formed between squash inhibitors and bovine trypsin. The ST-CMTI complex was formed from the reactive-site-cleaved form of the inhibitor. However, well defined electron density was observed for the P1-P1' peptide bond, together with a hydrogen-bonding pattern virtually identical to those of all serine-protease-protein-inhibitor complexes, indicating a resynthesis of the scissile bond.
机译：一个阴离子从大西洋鲑鱼和牛胰蛋白酶胰蛋白酶已经包裹着南瓜籽抑制剂,CMTI-I (Cucurbita maxima胰蛋白酶抑制剂,P1 Arg)和CPTI-II (Cucurbita浆果胰蛋白酶抑制剂二世,P1赖氨酸)。三个这样的复合物结构决心要1.5 - -1.8决议和改进晶体R因子从17.6到19.3%。(ST-CPTI和ST-CMTI)和bovine-trypsin复杂的(BT-CPTI)相对于其他胰蛋白酶抑制剂复合物的将军结构和主要和次要绑定特性。主要结合抑制剂结合的残渣胰蛋白酶古典的方式,但小差异主要和次要绑定模式。比赖氨酸特异性口袋里的牛胰蛋白酶在其他已知lysine-bovine-trypsin复合物,和阴离子鲑鱼胰蛋白酶缺乏一些二次绑定交互中发现的南瓜抑制剂之间形成复合物牛胰蛋白酶。从的reactive-site-cleaved形式抑制剂。观察P1-P1的肽键,与氢键模式几乎相同的serine-protease-protein-inhibitor复合物,指示的再合成易裂开的债券。

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