6W41
Crystal structure of SARS-CoV-2 receptor binding domain in complex with human antibody CR3022
Summary for 6W41
| Entry DOI | 10.2210/pdb6w41/pdb |
| Descriptor | CR3022 Fab heavy chain, CR3022 Fab light chain, Spike protein S1, ... (6 entities in total) |
| Functional Keywords | antibody, virus, complex, sars-cov-2, immune system, immune system-viral protein complex, immune system/viral protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 74433.16 |
| Authors | Yuan, M.,Wu, N.C.,Zhu, X.Y.,Wilson, I.A. (deposition date: 2020-03-09, release date: 2020-03-25, Last modification date: 2024-11-13) |
| Primary citation | Yuan, M.,Wu, N.C.,Zhu, X.,Lee, C.D.,So, R.T.Y.,Lv, H.,Mok, C.K.P.,Wilson, I.A. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science, 368:630-633, 2020 Cited by PubMed Abstract: The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2. PubMed: 32245784DOI: 10.1126/science.abb7269 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.084 Å) |
Structure validation
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