6533b826fe1ef96bd12850bd
RESEARCH PRODUCT
Structure of the 5′ untranslated region in SARS-CoV-2 genome and its specific recognition by innate immune systemviathe human oligoadenylate synthase 1
Emmanuelle BignonTom MiclotAlessio TerenziGiampaolo BaroneAntonio Monarisubject
Molecular dynamicSettore CHIM/03 - Chimica Generale E InorganicaSARS-CoV-2 infectionMaterials ChemistryMetals and AlloysCeramics and CompositesRNAGeneral Chemistrybiochemical phenomena metabolism and nutrition2′-5′-Oligoadenylate synthetase 1CatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialsdescription
2′-5′-Oligoadenylate synthetase 1 (OAS1) is one of the key enzymes driving the innate immune system response to SARS-CoV-2 infection whose activity has been related to COVID-19 severity. OAS1 is a sensor of endogenous RNA that triggers the 2′-5′-oligoadenylate/RNase L pathway. Upon SARS-CoV-2 infection, OAS1 is responsible for the recognition of viral RNA and has been shown to possess a particularly high sensitivity for the 5′-untranslated (5′-UTR) RNA region, which is organized in a double-strand stem loop motif (SL1). Here we report the structure of the SL1/OAS1 complex also rationalizing the high affinity for OAS1.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2022-01-01 | Chemical Communications |