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  • Structure of the 5 untranslated region in SARS-CoV-2 genome and its specific recognition by innate immune system via the human oligoadenylate synthase 1 #MMPMID35060977
  • Bignon E; Miclot T; Terenzi A; Barone G; Monari A
  • Chem Commun (Camb) 2022[Feb]; 58 (13): 2176-2179 PMID35060977show ga
  • 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.
  • |*Immunity, Innate[MESH]
  • |2',5'-Oligoadenylate Synthetase/*metabolism[MESH]
  • |5' Untranslated Regions[MESH]
  • |Base Sequence[MESH]
  • |Binding Sites[MESH]
  • |COVID-19/pathology/virology[MESH]
  • |Humans[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Nucleic Acid Conformation[MESH]
  • |RNA, Viral/chemistry/genetics/*metabolism[MESH]
  • |SARS-CoV-2/*genetics/isolation & purification[MESH]

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  • suck abstract from ncbi

    2176 13.58 2022