How a rotavirus hijacks the human protein synthesis machinery

被引：14

作者：

Varani, G ^{[1
]}

Allain, FHT

机构：

[1] Univ Washington, Dept Chem, Seattle, WA 98102 USA

[2] Univ Washington, Dept Biochem, Seattle, WA 98102 USA

[3] ETH Honggerberg, Inst Mol Biol & Biophys, HPK, Dept Biol, CH-8093 Zurich, Switzerland

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 03期

关键词：

D O I：

10.1038/nsb0302-158

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The NSP3 protein from rotaviruses recognizes a unique sequence at the 3' end of the rotaviral mRNA. By doing so, it promotes translation of viral proteins while repressing host protein synthesis. The structure of the NSP3 protein bound to a viral 3' end sequence reveals how this occurs and suggests how it might be possible to design a new class of antiviral drugs.

引用

页码：158 / 160

页数：3

共 25 条

[21] Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G [J].