蛋白酶-蛋白抑制剂相互作用。

Biomedica biochimica acta Pub Date : 1991-01-01
W Bode, R Huber
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引用次数: 0

摘要

直到最近,“小”丝氨酸蛋白酶抑制剂的“底物样”“典型”抑制和羧基肽酶抑制剂的“产物样”抑制为蛋白质抑制剂-蛋白酶相互作用提供了唯一的模型。最近发表的胱抑素/ stein -木瓜蛋白酶复合物和水蛭素-凝血酶复合物的结构揭示了仅部分底物样特征的相互作用的新模式。尽管在了解蛇蛋白的天然切割转变方面取得了相当大的进展,但它们与同源丝氨酸蛋白酶相互作用的机制仍然是一个猜想问题。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Proteinase-protein inhibitor interaction.

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.

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