The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
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DOI：
10.1016/s0092-8674(00)81350-1
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发表时间：
1996-10-18
期刊：
影响因子：
64.5
通讯作者：
Hostomska, Z
中科院分区：
文献类型：
--
作者：
Love, RA;Parge, HE;Hostomska, Z
在丙型肝炎病毒 (HCV) 复制过程中，多蛋白加工的最后步骤是由位于非结构蛋白 3 N 端三分之一处的病毒蛋白酶执行的。来自 HCV BK 株的 NS3 蛋白酶的结构通过 X 射线晶体学以 2.4 埃分辨率测定。 NS3P 作为胰蛋白酶样蛋白酶折叠，具有两个 β 桶和 His-57、Asp-81、Ser-139 催化三联体。该结构具有与酶的裂解特异性一致的底物结合位点。新颖的特征包括结构性锌结合位点和长 N 末端，该末端通过与疏水性表面斑块结合而与邻近分子相互作用。
During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 Angstrom resolution. NS3P folds as a trypsinlike proteinase with two beta barrels and a catalytic triad of His-57, Asp-81, Ser-139. The structure has a substrate-binding site consistent with the cleavage specificity of the enzyme. Novel features include a structural zinc-binding site and a long N-terminus that interacts with neighboring molecules by binding to a hydrophobic surface patch.