6XE1
Structure of SARS-CoV-2 spike protein receptor binding domain in complex with a potent neutralizing antibody, CV30 Fab
Summary for 6XE1
| Entry DOI | 10.2210/pdb6xe1/pdb |
| Descriptor | CV30 Fab Heavy chain, CV30 Fab Kappa chain, Spike protein S1, ... (5 entities in total) |
| Functional Keywords | antibody, covid-19, immune system, viral protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 77691.76 |
| Authors | Hurlburt, N.K.,Pancera, M. (deposition date: 2020-06-11, release date: 2020-07-01, Last modification date: 2024-10-09) |
| Primary citation | Hurlburt, N.K.,Seydoux, E.,Wan, Y.H.,Edara, V.V.,Stuart, A.B.,Feng, J.,Suthar, M.S.,McGuire, A.T.,Stamatatos, L.,Pancera, M. Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation. Nat Commun, 11:5413-5413, 2020 Cited by PubMed Abstract: SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2. PubMed: 33110068DOI: 10.1038/s41467-020-19231-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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