Turk V, Bode W
Department of Biochemistry, Jozef Stefan Institute, Ljubljana, Slovenia, Yugoslavia.
FEBS Lett. 1991 Jul 22;285(2):213-9. doi: 10.1016/0014-5793(91)80804-c.
The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, functions and evolutionary relationships. Although they differ in their molecular properties and biological distribution, they are structurally related proteins. All three inhibitory families, the stefins, the cystatins and the kininogens, are members of the same superfamily. Recently determined crystal structures of chicken cystatin and human stefin B established a new mechanism of interaction between cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinases and their inhibitors.
在过去十年中,半胱氨酸蛋白酶的蛋白质抑制剂在结构、功能和进化关系方面取得了巨大进展。尽管它们在分子特性和生物学分布上有所不同,但它们是结构相关的蛋白质。所有三个抑制家族,即丝抑蛋白、胱抑素和激肽原,都是同一超家族的成员。最近确定的鸡胱抑素和人丝抑蛋白B的晶体结构建立了半胱氨酸蛋白酶与其抑制剂之间的一种新的相互作用机制,这与丝氨酸蛋白酶及其抑制剂的标准机制有根本不同。