Serpins and other covalent protease inhibitors.
Serpins and other covalent protease inhibitors.
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DOI：
10.1016/s0959-440x(01)00275-5
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发表时间：
2001-12
影响因子：
6.8
通讯作者：
Sheng Ye;Elizabeth J. Goldsmith
中科院分区：
文献类型：
--
作者：
Sheng Ye;Elizabeth J. Goldsmith
丝氨酸蛋白酶抑制剂是不可逆的共价“自杀”蛋白酶抑制剂。在过去的两年中，丝氨酸蛋白酶抑制剂的结构生物学取得了重要进展，胰蛋白酶和α1-抗胰蛋白酶之间的共价复合物的晶体结构，以及胰蛋白酶S195A和来自Manduca sexta的丝氨酸蛋白酶抑制剂1B之间的米氏相遇复合物的晶体结构。这些结构有助于阐明丝氨酸蛋白酶抑制剂作用机制的许多方面。此外，半胱氨酸蛋白酶 caspase-8 与抑制剂 p35 复合物的晶体结构揭示了一个新的自杀蛋白酶抑制剂家族。
Serpins are irreversible covalent ‘suicide’ protease inhibitors. In the past two years, important advances in the structural biology of serpins have been forthcoming with the crystal structures of a covalent complex between trypsin and α1-antitrypsin, and of a Michaelis encounter complex between trypsin S195A and serpin 1B from Manduca sexta. These structures have helped elucidate many aspects of the mechanism of action of serpins. Also, the crystal structure of the cysteine protease caspase-8 in complex with the inhibitor p35 has revealed a new family of suicide protease inhibitors.