MODE OF ACTION OF SOYBEAN TRYPSIN-INHIBITOR (KUNITZ) AS A MODEL FOR SPECIFIC PROTEIN-PROTEIN INTERACTIONS
MODE OF ACTION OF SOYBEAN TRYPSIN-INHIBITOR (KUNITZ) AS A MODEL FOR SPECIFIC PROTEIN-PROTEIN INTERACTIONS
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DOI：
10.1038/249054a0
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发表时间：
1974-01-01
期刊：
影响因子：
64.8
通讯作者：
SWEET, RM
中科院分区：
文献类型：
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作者：
BLOW, DM;JANIN, J;SWEET, RM
蛋白质胰蛋白酶抑制剂是与胰蛋白酶结合非常强烈的蛋白质，阻断其活性位点（Ki= 10− 9至10− 14 M）我们对大豆胰蛋白酶抑制剂（Kunitz）（STI）（最大的抑制剂之一）与猪胰蛋白酶的复合物进行了晶体结构分析。Huber和他的同事已经确定了一种小抑制剂，牛胰蛋白酶抑制剂（Kunitz）（PTI）与牛胰蛋白酶1的复合物的结构。这些研究提高了我们对胰蛋白酶催化机制的理解，证明了各种胰蛋白酶抑制剂以类似的方式起作用，并为蛋白质分子之间强特异性结合的发展提供了见解。
THE protein trypsin inhibitors are proteins which bind very strongly to trypsin, blocking its active site (Ki= 10−9to 10−14M) we have carried out a crystal structure analysis of the complex of soybean trypsin inhibitor (Kunitz) (STI), one of the largest inhibitors, with porcine trypsin. Huber and his colleagues have determined the structure of a complex of a small inhibitor, bovine pancreatic trypsin inhibitor (Kunitz) (PTI), with bovine trypsin1. These studies improve our understanding of the catalytic mechanism of trypsin, demonstrate that various trypsin inhibitors act in a similar way and provide insight into the development of strong, specific binding between protein molecules.