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Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
Published on: May 13, 2019
Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex.
James Chen1, Brandon Malone1, Eliza Llewellyn1
1Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY, 10065 USA.
Structural insights reveal how SARS-CoV-2 RNA polymerase and helicase interact, essential for viral replication. This finding offers new targets for COVID-19 antiviral therapies.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) causes the ongoing COVID-19 pandemic.
- Viral replication relies on the RNA-dependent RNA polymerase (RdRp) holoenzyme and accessory factors, including the nsp13 helicase.
- Both the RdRp holoenzyme and nsp13 are crucial for viral replication and represent key targets for antiviral drug development.
Conclusions:
- The determined structures provide critical insights into the functional interplay between the SARS-CoV-2 RdRp holoenzyme and the nsp13 helicase.
- The identification of a novel binding pocket on nsp12 offers a promising avenue for the design of new antiviral drugs targeting SARS-CoV-2 replication.
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