7JJJ
Structure of SARS-CoV-2 3Q-2P full-length dimers of spike trimers
This is a non-PDB format compatible entry.
Summary for 7JJJ
| Entry DOI | 10.2210/pdb7jjj/pdb |
| EMDB information | 22354 |
| 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-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | sars-cov-2, glycoprotein, immunogen, vaccine, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 6 |
| Total formula weight | 885457.00 |
| Authors | Bangaru, S.,Turner, H.L.,Ozorowski, G.,Antanasijevic, A.,Ward, A.B. (deposition date: 2020-07-26, release date: 2020-08-26, Last modification date: 2024-11-06) |
| Primary citation | Bangaru, S.,Ozorowski, G.,Turner, H.L.,Antanasijevic, A.,Huang, D.,Wang, X.,Torres, J.L.,Diedrich, J.K.,Tian, J.H.,Portnoff, A.D.,Patel, N.,Massare, M.J.,Yates 3rd, J.R.,Nemazee, D.,Paulson, J.C.,Glenn, G.,Smith, G.,Ward, A.B. Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate. Science, 370:1089-1094, 2020 Cited by PubMed Abstract: Vaccine efforts to combat the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is responsible for the current coronavirus disease 2019 (COVID-19) pandemic, are focused on SARS-CoV-2 spike glycoprotein, the primary target for neutralizing antibodies. We performed cryo-election microscopy and site-specific glycan analysis of one of the leading subunit vaccine candidates from Novavax, which is based on a full-length spike protein formulated in polysorbate 80 detergent. Our studies reveal a stable prefusion conformation of the spike immunogen with slight differences in the S1 subunit compared with published spike ectodomain structures. We also observed interactions between the spike trimers, allowing formation of higher-order spike complexes. This study confirms the structural integrity of the full-length spike protein immunogen and provides a basis for interpreting immune responses to this multivalent nanoparticle immunogen. PubMed: 33082295DOI: 10.1126/science.abe1502 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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