一个点突变消除了丙型肝炎病毒NS3蛋白的解旋酶活性，但未消除其三磷酸核苷酶活性。
A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein.
作者信息
Heilek G M, Peterson M G
机构信息
Tularik Inc., South San Francisco, California 94080, USA.
出版信息
J Virol. 1997 Aug;71(8):6264-6. doi: 10.1128/JVI.71.8.6264-6266.1997.
Abstract
The NS3 protein of hepatitis C virus contains a bipartite structure consisting of an N-terminal serine protease and a C-terminal DEAD box helicase. We show that the C-terminal domain has ATPase and panhelicase activities. The integrity of the helicase function is dependent on the conserved DEAD motif and can be abolished by a His-Ala point mutation, leaving a fully functional nucleoside triphosphatase.
摘要
丙型肝炎病毒的NS3蛋白包含一个由N端丝氨酸蛋白酶和C端DEAD盒解旋酶组成的双结构。我们发现C端结构域具有ATP酶和泛解旋酶活性。解旋酶功能的完整性依赖于保守的DEAD基序，并且可以通过组氨酸-丙氨酸点突变消除，从而留下一个功能完全正常的核苷三磷酸酶。
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