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-Structure paper
Title | The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 118, Issue 9, Year 2021 |
Publish date | Mar 2, 2021 |
Authors | Donald J Benton / Antoni G Wrobel / Chloë Roustan / Annabel Borg / Pengqi Xu / Stephen R Martin / Peter B Rosenthal / John J Skehel / Steven J Gamblin / |
PubMed Abstract | 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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:33579792 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 - 4.2 Å |
Structure data | EMDB-12229, PDB-7bnm: EMDB-12230, PDB-7bnn: EMDB-12231, PDB-7bno: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN / Spike / SARS-CoV-2 |