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10.1038/s41467-020-17371-6

http://scihub22266oqcxt.onion/10.1038/s41467-020-17371-6
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32681106!7367865!32681106
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suck abstract from ncbi


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pmid32681106      Nat+Commun 2020 ; 11 (1): 3618
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  • Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein #MMPMID32681106
  • Fan X; Cao D; Kong L; Zhang X
  • Nat Commun 2020[Jul]; 11 (1): 3618 PMID32681106show ga
  • Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses.
  • |Amino Acid Motifs[MESH]
  • |Betacoronavirus/*chemistry/*physiology[MESH]
  • |COVID-19[MESH]
  • |Coronavirus Infections/virology[MESH]
  • |Coronavirus/chemistry/classification[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Humans[MESH]
  • |Membrane Fusion[MESH]
  • |Models, Molecular[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/virology[MESH]
  • |Protein Conformation[MESH]
  • |Protein Multimerization[MESH]
  • |SARS-CoV-2[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry[MESH]


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