Distinct conformational states of SARS-CoV-2 spike protein
pmc: PMC7464562 , PMC7263552
Distinct conformational states of SARS-CoV-2 spike protein
A dynamic viral spike Efforts to protect human cells against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have focused on the trimeric spike (S) protein. Several structures have shown a stabilized ectodomain of the spike in its prefusion conformation. Cai et al. now provide insight into the structural changes in the S protein that result in the fusion of the viral and host cell membranes. They purified full-length S protein and determined cryo–electron microscopy structures of both the prefusion and postfusion conformations. These structures add to our understanding of S protein function and could inform vaccine design. Science , this issue p. 1586
- Boston Children's Hospital United States
- Harvard University United States
Cryoelectron Microscopy, Peptidyl-Dipeptidase A, Virus Internalization, Protein Structure, Secondary, HEK293 Cells, Protein Domains, Host-Pathogen Interactions, Spike Glycoprotein, Coronavirus, Humans, Receptors, Virus, Angiotensin-Converting Enzyme 2, Protein Multimerization, Research Articles
Cryoelectron Microscopy, Peptidyl-Dipeptidase A, Virus Internalization, Protein Structure, Secondary, HEK293 Cells, Protein Domains, Host-Pathogen Interactions, Spike Glycoprotein, Coronavirus, Humans, Receptors, Virus, Angiotensin-Converting Enzyme 2, Protein Multimerization, Research Articles
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