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Nature Structural Biology  9, 158 - 160 (2002)
doi:10.1038/nsb0302-158

How a rotavirus hijacks the human protein synthesis machinery

Gabriele Varani1 & Frédéric H.-T. Allain2

1  Gabriele Varani is in the Departments of Chemistry and Biochemistry, University of Washington, Seattle Washington 98102-1700, USA.

2  Frédéric H.-T. Allain is at ETH Zurich, Department of Biology, Institut fur Molekularbiologie und Biophysik, ETH Honggerberg, HPK, CH-8093 Zurich, Switzerland.

Correspondence should be addressed to Gabriele Varani varani@chem.washington.edu or Frédéric H.-T. Allain allain@mol.biol.ethz.ch
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.

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RESEARCH
Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F
The EMBO Journal Article (01 Oct 1998)

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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