6VSB
Prefusion 2019-nCoV spike glycoprotein with a single receptor-binding domain up
Summary for 6VSB
| Entry DOI | 10.2210/pdb6vsb/pdb |
| EMDB information | 21374 21375 |
| Descriptor | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | spike, fusion glycoprotein, coronavirus, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 3 |
| Total formula weight | 440385.56 |
| Authors | Wrapp, D.,Wang, N.,Corbett, K.S.,Goldsmith, J.A.,Hsieh, C.,Abiona, O.,Graham, B.S.,McLellan, J.S. (deposition date: 2020-02-10, release date: 2020-02-26, Last modification date: 2024-10-23) |
| Primary citation | Wrapp, D.,Wang, N.,Corbett, K.S.,Goldsmith, J.A.,Hsieh, C.L.,Abiona, O.,Graham, B.S.,McLellan, J.S. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science, 367:1260-1263, 2020 Cited by PubMed Abstract: The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis. PubMed: 32075877DOI: 10.1126/science.abb2507 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.46 Å) |
Structure validation
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