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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Fuguo Jiang & Anand Ramanathan & Matthew T. Miller & Guo-Qing Tang & Michael Gale & Smita S. Patel & Joseph Marcotrigiano, 2011. "Structural basis of RNA recognition and activation by innate immune receptor RIG-I," Nature, Nature, vol. 479(7373), pages 423-427, November.
    • Handle: RePEc:nat:nature:v:479:y:2011:i:7373:d:10.1038_nature10537
    DOI: 10.1038/nature10537
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    Cited by:

    1. Qin Yu & Alba Herrero del Valle & Rahul Singh & Yorgo Modis, 2021. "MDA5 disease variant M854K prevents ATP-dependent structural discrimination of viral and cellular RNA," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

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