6M3W
Post-fusion structure of SARS-CoV spike glycoprotein
Summary for 6M3W
| Entry DOI | 10.2210/pdb6m3w/pdb |
| EMDB information | 30072 |
| Descriptor | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | spike, post-fusion, sars-cov, coronavirus, glycoprotein, trimer, viral protein |
| Biological source | Human SARS coronavirus (SARS-CoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 167585.36 |
| Authors | |
| Primary citation | Fan, X.,Cao, D.,Kong, L.,Zhang, X. Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein. Nat Commun, 11:3618-3618, 2020 Cited by PubMed Abstract: 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. PubMed: 32681106DOI: 10.1038/s41467-020-17371-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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