7TLY
SARS-CoV-2 S B.1.1.529 Omicron variant (RBD + S309 Local Refinement)
Summary for 7TLY
| Entry DOI | 10.2210/pdb7tly/pdb |
| Related | 7TLY 7TLZ 7TM0 7TN0 |
| EMDB information | 25990 25991 25992 25993 |
| Descriptor | S309 Fab heavy chain, S309 Fab light chain, Spike glycoprotein, ... (4 entities in total) |
| Functional Keywords | omicron, receptor-binding domain, sars-cov-2, covid, b.1.529, rbd, antibody, fab, s309, sotrovimab, structural genomics, seattle structural genomics center for infectious disease, ssgcid, virus-immune system complex, virus/immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 179456.15 |
| Authors | McCallum, M.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2022-01-19, release date: 2022-02-02, Last modification date: 2024-11-06) |
| Primary citation | McCallum, M.,Czudnochowski, N.,Rosen, L.E.,Zepeda, S.K.,Bowen, J.E.,Walls, A.C.,Hauser, K.,Joshi, A.,Stewart, C.,Dillen, J.R.,Powell, A.E.,Croll, T.I.,Nix, J.,Virgin, H.W.,Corti, D.,Snell, G.,Veesler, D. Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement. Science, 375:864-868, 2022 Cited by PubMed Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus. PubMed: 35076256DOI: 10.1126/science.abn8652 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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