7DK3
SARS-CoV-2 S trimer, S-open
Summary for 7DK3
| Entry DOI | 10.2210/pdb7dk3/pdb |
| EMDB information | 30701 |
| Descriptor | Spike glycoprotein (1 entity in total) |
| Functional Keywords | spike glycoprotein, coronavirus, sars-cov-2 virus, covid-19, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 420167.72 |
| Authors | |
| Primary citation | Xu, C.,Wang, Y.,Liu, C.,Zhang, C.,Han, W.,Hong, X.,Wang, Y.,Hong, Q.,Wang, S.,Zhao, Q.,Wang, Y.,Yang, Y.,Chen, K.,Zheng, W.,Kong, L.,Wang, F.,Zuo, Q.,Huang, Z.,Cong, Y. Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: The recent outbreaks of SARS-CoV-2 pose a global health emergency. The SARS-CoV-2 trimeric spike (S) glycoprotein interacts with the human ACE2 receptor to mediate viral entry into host cells. We report the cryo-EM structures of a tightly closed SARS-CoV-2 S trimer with packed fusion peptide and an ACE2-bound S trimer at 2.7- and 3.8-Å resolution, respectively. Accompanying ACE2 binding to the up receptor-binding domain (RBD), the associated ACE2-RBD exhibits continuous swing motions. Notably, the SARS-CoV-2 S trimer appears much more sensitive to the ACE2 receptor than the SARS-CoV S trimer regarding receptor-triggered transformation from the closed prefusion state to the fusion-prone open state, potentially contributing to the superior infectivity of SARS-CoV-2. We defined the RBD T470-T478 loop and Y505 as viral determinants for specific recognition of SARS-CoV-2 RBD by ACE2. Our findings depict the mechanism of ACE2-induced S trimer conformational transitions from the ground prefusion state toward the postfusion state, facilitating development of anti-SARS-CoV-2 vaccines and therapeutics. PubMed: 33277323DOI: 10.1126/sciadv.abe5575 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6 Å) |
Structure validation
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