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10.1073/pnas.2021785118

http://scihub22266oqcxt.onion/10.1073/pnas.2021785118
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33361333!7812859!33361333
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suck abstract from ncbi


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pmid33361333      Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (2): ä
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  • Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein #MMPMID33361333
  • Flower TG; Buffalo CZ; Hooy RM; Allaire M; Ren X; Hurley JH
  • Proc Natl Acad Sci U S A 2021[Jan]; 118 (2): ä PMID33361333show ga
  • The molecular basis for the severity and rapid spread of the COVID-19 disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely unknown. ORF8 is a rapidly evolving accessory protein that has been proposed to interfere with immune responses. The crystal structure of SARS-CoV-2 ORF8 was determined at 2.04-A resolution by X-ray crystallography. The structure reveals a approximately 60-residue core similar to SARS-CoV-2 ORF7a, with the addition of two dimerization interfaces unique to SARS-CoV-2 ORF8. A covalent disulfide-linked dimer is formed through an N-terminal sequence specific to SARS-CoV-2, while a separate noncovalent interface is formed by another SARS-CoV-2-specific sequence, (73)YIDI(76) Together, the presence of these interfaces shows how SARS-CoV-2 ORF8 can form unique large-scale assemblies not possible for SARS-CoV, potentially mediating unique immune suppression and evasion activities.
  • |*Molecular Structure[MESH]
  • |Evolution, Molecular[MESH]
  • |Immune Evasion[MESH]
  • |SARS-CoV-2/*chemistry[MESH]


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