7JVB
Crystal structure of the SARS-CoV-2 spike receptor-binding domain (RBD) with nanobody Nb20
Summary for 7JVB
| Entry DOI | 10.2210/pdb7jvb/pdb |
| Descriptor | Spike protein S1, Nanobody Nb20, CACODYLATE ION (3 entities in total) |
| Functional Keywords | sars-cov-2, covid-19, nanobody, spike protein, receptor-binding domain, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2, COVID-19 virus) More |
| Total number of polymer chains | 4 |
| Total formula weight | 76012.83 |
| Authors | |
| Primary citation | Xiang, Y.,Nambulli, S.,Xiao, Z.,Liu, H.,Sang, Z.,Duprex, W.P.,Schneidman-Duhovny, D.,Zhang, C.,Shi, Y. Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2. Science, 370:1479-1484, 2020 Cited by PubMed Abstract: Cost-effective, efficacious therapeutics are urgently needed to combat the COVID-19 pandemic. In this study, we used camelid immunization and proteomics to identify a large repertoire of highly potent neutralizing nanobodies (Nbs) to the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein receptor binding domain (RBD). We discovered Nbs with picomolar to femtomolar affinities that inhibit viral infection at concentrations below the nanograms-per-milliliter level, and we determined a structure of one of the most potent Nbs in complex with the RBD. Structural proteomics and integrative modeling revealed multiple distinct and nonoverlapping epitopes and indicated an array of potential neutralization mechanisms. We bioengineered multivalent Nb constructs that achieved ultrahigh neutralization potency (half-maximal inhibitory concentration as low as 0.058 ng/ml) and may prevent mutational escape. These thermostable Nbs can be rapidly produced in bulk from microbes and resist lyophilization and aerosolization. PubMed: 33154108DOI: 10.1126/science.abe4747 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.287 Å) |
Structure validation
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