{"title":"蛋白酶-蛋白抑制剂相互作用。","authors":"W Bode, R Huber","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Until recently, the \"substrate-like\" \"canonical\" inhibition by the \"small\" serine proteinase inhibitors, and the product-like inhibition by the carboxypeptidase inhibitor, provided the only models for protein inhibitor-proteinase interactions. The recently published structures of cystatin/stefin-papain complexes and of hirudin-thrombin complexes reveal novel modes of interactions of only partial substrate-like character. Despite considerable progress in understanding the native-cleaved transition of the serpins, the mechanisms of their interaction with their cognate serine proteinases is still a matter of conjecture.</p>","PeriodicalId":8948,"journal":{"name":"Biomedica biochimica acta","volume":"50 4-6","pages":"437-46"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Proteinase-protein inhibitor interaction.\",\"authors\":\"W Bode, R Huber\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Until recently, the \\\"substrate-like\\\" \\\"canonical\\\" inhibition by the \\\"small\\\" serine proteinase inhibitors, and the product-like inhibition by the carboxypeptidase inhibitor, provided the only models for protein inhibitor-proteinase interactions. The recently published structures of cystatin/stefin-papain complexes and of hirudin-thrombin complexes reveal novel modes of interactions of only partial substrate-like character. Despite considerable progress in understanding the native-cleaved transition of the serpins, the mechanisms of their interaction with their cognate serine proteinases is still a matter of conjecture.</p>\",\"PeriodicalId\":8948,\"journal\":{\"name\":\"Biomedica biochimica acta\",\"volume\":\"50 4-6\",\"pages\":\"437-46\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomedica biochimica acta\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomedica biochimica acta","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Until recently, the "substrate-like" "canonical" inhibition by the "small" serine proteinase inhibitors, and the product-like inhibition by the carboxypeptidase inhibitor, provided the only models for protein inhibitor-proteinase interactions. The recently published structures of cystatin/stefin-papain complexes and of hirudin-thrombin complexes reveal novel modes of interactions of only partial substrate-like character. Despite considerable progress in understanding the native-cleaved transition of the serpins, the mechanisms of their interaction with their cognate serine proteinases is still a matter of conjecture.