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-Structure paper
Title | Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication. |
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Journal, issue, pages | Mol Cell, Vol. 81, Issue 7, Page 1548-11552.e4, Year 2021 |
Publish date | Apr 1, 2021 |
Authors | Jack P K Bravo / Tyler L Dangerfield / David W Taylor / Kenneth A Johnson / |
PubMed Abstract | Remdesivir is a nucleoside analog approved by the US FDA for treatment of COVID-19. Here, we present a 3.9-Å-resolution cryo-EM reconstruction of a remdesivir-stalled RNA-dependent RNA polymerase ...Remdesivir is a nucleoside analog approved by the US FDA for treatment of COVID-19. Here, we present a 3.9-Å-resolution cryo-EM reconstruction of a remdesivir-stalled RNA-dependent RNA polymerase complex, revealing full incorporation of 3 copies of remdesivir monophosphate (RMP) and a partially incorporated fourth RMP in the active site. The structure reveals that RMP blocks RNA translocation after incorporation of 3 bases following RMP, resulting in delayed chain termination, which can guide the rational design of improved antiviral drugs. |
External links | Mol Cell / PubMed:33631104 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.89 Å |
Structure data | EMDB-23109, PDB-7l1f: |
Source |
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Keywords | VIRAL PROTEIN/RNA / VIRAL PROTEIN / VIRAL PROTEIN-RNA complex |