6NB4
MERS-CoV S complex with human neutralizing LCA60 antibody Fab fragment (state 2)
Summary for 6NB4
| Entry DOI | 10.2210/pdb6nb4/pdb |
| Related | 6NB3 6NB5 6NB6 6NB7 6NB8 |
| EMDB information | 0401 0402 0403 0404 |
| Descriptor | Spike glycoprotein, LCA60 heavy chain, LCA60 light chain, ... (9 entities in total) |
| Functional Keywords | coronavirus spike glycoprotein, mers-cov, sars-cov, human neutralizing antibodies, structural genomics, seattle structural genomics center for infectious disease, ssgcid, virus |
| Biological source | Middle East respiratory syndrome coronavirus More |
| Total number of polymer chains | 5 |
| Total formula weight | 495354.19 |
| Authors | Walls, A.C.,Xiong, X.,Park, Y.J.,Tortorici, M.A.,Snijder, S.,Quispe, J.,Cameroni, E.,Gopal, R.,Mian, D.,Lanzavecchia, A.,Zambon, M.,Rey, F.A.,Corti, D.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2018-12-06, release date: 2019-02-06, Last modification date: 2024-10-23) |
| Primary citation | Walls, A.C.,Xiong, X.,Park, Y.J.,Tortorici, M.A.,Snijder, J.,Quispe, J.,Cameroni, E.,Gopal, R.,Dai, M.,Lanzavecchia, A.,Zambon, M.,Rey, F.A.,Corti, D.,Veesler, D. Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell, 176:1026-1039.e15, 2019 Cited by PubMed Abstract: Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism. PubMed: 30712865DOI: 10.1016/j.cell.2018.12.028 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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