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Structural basis of an essential interaction between influenza polymerase and Pol II CTD

Author

Listed:
  • Maria Lukarska

    (European Molecular Biology Laboratory, Grenoble Outstation)

  • Guillaume Fournier

    (Institut Pasteur, Unité de Génétique Moléculaire des Virus à ARN
    CNRS, UMR3569
    Université Paris Diderot, Sorbonne Paris Cité, Unité de Génétique Moléculaire des Virus à ARN)

  • Alexander Pflug

    (European Molecular Biology Laboratory, Grenoble Outstation)

  • Patricia Resa-Infante

    (European Molecular Biology Laboratory, Grenoble Outstation)

  • Stefan Reich

    (European Molecular Biology Laboratory, Grenoble Outstation)

  • Nadia Naffakh

    (Institut Pasteur, Unité de Génétique Moléculaire des Virus à ARN
    CNRS, UMR3569
    Université Paris Diderot, Sorbonne Paris Cité, Unité de Génétique Moléculaire des Virus à ARN)

  • Stephen Cusack

    (European Molecular Biology Laboratory, Grenoble Outstation)

Abstract

The crystal structure of bat influenza A polymerase bound to a serine-5 phosphorylated peptide mimic from the C-terminal domain of cellular RNA polymerase II shows how the two polymerases are directly coupled and suggests that the interaction site could be targeted for antiviral drug development.

Suggested Citation

  • Maria Lukarska & Guillaume Fournier & Alexander Pflug & Patricia Resa-Infante & Stefan Reich & Nadia Naffakh & Stephen Cusack, 2017. "Structural basis of an essential interaction between influenza polymerase and Pol II CTD," Nature, Nature, vol. 541(7635), pages 117-121, January.
  • Handle: RePEc:nat:nature:v:541:y:2017:i:7635:d:10.1038_nature20594
    DOI: 10.1038/nature20594
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