Nature Communications (Aug 2021)

Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase

  • Joseph A. Newman,
  • Alice Douangamath,
  • Setayesh Yadzani,
  • Yuliana Yosaatmadja,
  • Antony Aimon,
  • José Brandão-Neto,
  • Louise Dunnett,
  • Tyler Gorrie-stone,
  • Rachael Skyner,
  • Daren Fearon,
  • Matthieu Schapira,
  • Frank von Delft,
  • Opher Gileadi

DOI
https://doi.org/10.1038/s41467-021-25166-6
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 11

Abstract

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The SARS-CoV-2 NSP13 helicase is essential for viral replication and of interest as a drug target. Here, the authors present the crystal structures of NSP13 in the apo form and bound to either phosphate or the non-hydrolysable ATP analog AMP-PNP and discuss the helicase mechanism. They also perform a crystallographic fragment screening and identify 65 bound fragments, which could help in the design of new antiviral agents.