Structural basis of RNA recognition and activation by innate immune receptor RIG-I

Fuguo Jiang, Anand Ramanathan, Matthew T. Miller, Guo-Qing Tang, Michael Gale, Smita S. Patel () and Joseph Marcotrigiano ()
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Fuguo Jiang: Center for Advanced Biotechnology and Medicine, Rutgers University, 679 Hoes Lane West, Piscataway, New Jersey 08854, USA
Anand Ramanathan: UMDNJ-RWJ Medical School, 675 Hoes Lane West, Piscataway, New Jersey 08854, USA
Matthew T. Miller: Center for Advanced Biotechnology and Medicine, Rutgers University, 679 Hoes Lane West, Piscataway, New Jersey 08854, USA
Guo-Qing Tang: UMDNJ-RWJ Medical School, 675 Hoes Lane West, Piscataway, New Jersey 08854, USA
Michael Gale: University of Washington School of Medicine, 1959 NE Pacific Street, Seattle, Washington 98195, USA
Smita S. Patel: UMDNJ-RWJ Medical School, 675 Hoes Lane West, Piscataway, New Jersey 08854, USA
Joseph Marcotrigiano: Center for Advanced Biotechnology and Medicine, Rutgers University, 679 Hoes Lane West, Piscataway, New Jersey 08854, USA

Nature, 2011, vol. 479, issue 7373, 423-427

Abstract: Virus-binding helicase structure The binding of helicase to viral RNA and the resulting activation of the retinoic acid inducible gene-I (RIG-I) are central to the innate immune response to viral infection. The structure of the RIG-I helicase domain with its repressor domain, in complex with double-stranded RNA, has now been determined. The structure suggests a mechanism of dsRNA translocation. Because RIG-I is homologous to many other helicases, such as Dicer of the RNAi machinery and the FANCM helicases involved in DNA repair, the structure should prove relevant to helicases in these other biological processes.

Date: 2011
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DOI: 10.1038/nature10537

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