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10.1073/pnas.2022586118

http://scihub22266oqcxt.onion/10.1073/pnas.2022586118
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33579792!7936381!33579792
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suck abstract from ncbi


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pmid33579792      Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (9): ä
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  • The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2 #MMPMID33579792
  • Benton DJ; Wrobel AG; Roustan C; Borg A; Xu P; Martin SR; Rosenthal PB; Skehel JJ; Gamblin SJ
  • Proc Natl Acad Sci U S A 2021[Mar]; 118 (9): ä PMID33579792show ga
  • The majority of currently circulating severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viruses have mutant spike glycoproteins that contain the D614G substitution. Several studies have suggested that spikes with this substitution are associated with higher virus infectivity. We use cryo-electron microscopy to compare G614 and D614 spikes and show that the G614 mutant spike adopts a range of more open conformations that may facilitate binding to the SARS-CoV-2 receptor, ACE2, and the subsequent structural rearrangements required for viral membrane fusion.
  • |COVID-19/*virology[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Humans[MESH]
  • |Protein Conformation[MESH]
  • |SARS-CoV-2/*chemistry/genetics[MESH]
  • |Spike Glycoprotein, Coronavirus/*chemistry/genetics[MESH]


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