7SOD
SARS-CoV-2 S NTD B.1.617.1 kappa variant S2L20 Local Refinement
Summary for 7SOD
| Entry DOI | 10.2210/pdb7sod/pdb |
| EMDB information | 25267 |
| Descriptor | S2L20 Fab light chain, S2L20 Fab heavy chain, Spike glycoprotein, ... (5 entities in total) |
| Functional Keywords | kappa, spike, antibody, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein-immune system complex, viral protein/immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 168680.85 |
| Authors | McCallum, M.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2021-10-29, release date: 2021-11-17, Last modification date: 2024-10-23) |
| Primary citation | McCallum, M.,Walls, A.C.,Sprouse, K.R.,Bowen, J.E.,Rosen, L.E.,Dang, H.V.,De Marco, A.,Franko, N.,Tilles, S.W.,Logue, J.,Miranda, M.C.,Ahlrichs, M.,Carter, L.,Snell, G.,Pizzuto, M.S.,Chu, H.Y.,Van Voorhis, W.C.,Corti, D.,Veesler, D. Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants. Science, 374:1621-1626, 2021 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) transmission leads to the emergence of variants, including the B.1.617.2 (Delta) variant of concern that is causing a new wave of infections and has become globally dominant. We show that these variants dampen the in vitro potency of vaccine-elicited serum neutralizing antibodies and provide a structural framework for describing their immune evasion. Mutations in the B.1.617.1 (Kappa) and Delta spike glycoproteins abrogate recognition by several monoclonal antibodies via alteration of key antigenic sites, including remodeling of the Delta amino-terminal domain. The angiotensin-converting enzyme 2 binding affinities of the Kappa and Delta receptor binding domains are comparable to the Wuhan-Hu-1 isolate, whereas B.1.617.2+ (Delta+) exhibits markedly reduced affinity. PubMed: 34751595DOI: 10.1126/science.abl8506 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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