7B17
SARS-CoV-spike RBD bound to two neutralising nanobodies.
Summary for 7B17
| Entry DOI | 10.2210/pdb7b17/pdb |
| EMDB information | 11980 |
| Descriptor | Spike protein S1, SARS-CoV-2 neutralizing biparatopic nanobody VE,nanobody E from Lama glama,SARS-CoV-2 neutralizing biparatopic nanobody VE,nanobody E from Lama glama, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | spike glycoprotein, sars-cov-2, nanobody, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
| Total number of polymer chains | 2 |
| Total formula weight | 52225.58 |
| Authors | Hallberg, B.M.,Das, H. (deposition date: 2020-11-23, release date: 2021-02-10, Last modification date: 2024-10-23) |
| Primary citation | Koenig, P.A.,Das, H.,Liu, H.,Kummerer, B.M.,Gohr, F.N.,Jenster, L.M.,Schiffelers, L.D.J.,Tesfamariam, Y.M.,Uchima, M.,Wuerth, J.D.,Gatterdam, K.,Ruetalo, N.,Christensen, M.H.,Fandrey, C.I.,Normann, S.,Todtmann, J.M.P.,Pritzl, S.,Hanke, L.,Boos, J.,Yuan, M.,Zhu, X.,Schmid-Burgk, J.L.,Kato, H.,Schindler, M.,Wilson, I.A.,Geyer, M.,Ludwig, K.U.,Hallberg, B.M.,Wu, N.C.,Schmidt, F.I. Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape Science, 371:-, 2021 Cited by PubMed Abstract: The pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread, with devastating consequences. For passive immunization efforts, nanobodies have size and cost advantages over conventional antibodies. In this study, we generated four neutralizing nanobodies that target the receptor binding domain of the SARS-CoV-2 spike protein. We used x-ray crystallography and cryo-electron microscopy to define two distinct binding epitopes. On the basis of these structures, we engineered multivalent nanobodies with more than 100 times the neutralizing activity of monovalent nanobodies. Biparatopic nanobody fusions suppressed the emergence of escape mutants. Several nanobody constructs neutralized through receptor binding competition, whereas other monovalent and biparatopic nanobodies triggered aberrant activation of the spike fusion machinery. These premature conformational changes in the spike protein forestalled productive fusion and rendered the virions noninfectious. PubMed: 33436526DOI: 10.1126/science.abe6230 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.01 Å) |
Structure validation
Download full validation report
