Pizzi E, Tramontano A, Tomei L, La Monica N, Failla C, Sardana M, Wood T, De Francesco R
Istituto di Ricerche di Biologia Molecolare, Rome, Italy.
Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):888-92. doi: 10.1073/pnas.91.3.888.
We have built a model of the specificity pocket of the protease of hepatitis C virus on the basis of the known structures of trypsin-like serine proteases and of the conservation pattern of the protease sequences among various hepatitis C strains. The model allowed us to predict that the substrate of this protease should have a cysteine residue in position P1. This hypothesis was subsequently proved by N-terminal sequencing of two products of the protease. The success of this "blind" test increases our confidence in the overall correctness of our proposed alignment of the enzyme sequence with those of other proteases of known structure and constitutes a first step in the construction of a complete model of the viral protease domain.
我们基于胰蛋白酶样丝氨酸蛋白酶的已知结构以及不同丙型肝炎病毒株中蛋白酶序列的保守模式，构建了丙型肝炎病毒蛋白酶特异性口袋的模型。该模型使我们能够预测这种蛋白酶的底物在P1位置应有一个半胱氨酸残基。这一假设随后通过对该蛋白酶的两种产物进行N端测序得到了证实。这次“盲测”的成功增强了我们对所提出的该酶序列与其他已知结构蛋白酶序列比对整体正确性的信心，并构成了构建病毒蛋白酶结构域完整模型的第一步。
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