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

Maria Lukarska, Guillaume Fournier, Alexander Pflug, Patricia Resa-Infante, Stefan Reich, Nadia Naffakh and Stephen Cusack ()
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Maria Lukarska: European Molecular Biology Laboratory, Grenoble Outstation
Guillaume Fournier: Institut Pasteur, 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
Stephen Cusack: European Molecular Biology Laboratory, Grenoble Outstation

Nature, 2017, vol. 541, issue 7635, 117-121

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.

Date: 2017
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DOI: 10.1038/nature20594

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