A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein

被引：59

作者：

Heilek, GM ^{[1
]}

Peterson, MG ^{[1
]}

机构：

[1] TULARIK INC, San Francisco, CA 94080 USA

来源：

JOURNAL OF VIROLOGY | 1997年 / 71卷 / 08期

关键词：

D O I：

10.1128/JVI.71.8.6264-6266.1997

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The NS3 protein of hepatitis C virus contains a bipartite structure consisting of an N-terminal serine pro tease and a C-terminal DEAD bos 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.

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页码：6264 / 6266

页数：3

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