6OE5
Splayed open prefusion RSV F captured by CR9501 and motavizumab Fabs
Summary for 6OE5
| Entry DOI | 10.2210/pdb6oe5/pdb |
| Descriptor | Fusion glycoprotein F0,Fibritin, Motavizumab Fab Heavy Chain, Motavizumab Fab Light Chain, ... (5 entities in total) |
| Functional Keywords | class i fusion glycoprotein, immunoglobulin, respiratory syncytial virus, trimerization, neutralizing, viral protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Human respiratory syncytial virus A (strain A2) More |
| Total number of polymer chains | 5 |
| Total formula weight | 156729.87 |
| Authors | Gilman, M.S.A.,McLellan, J.S. (deposition date: 2019-03-27, release date: 2019-04-17, Last modification date: 2024-11-06) |
| Primary citation | Gilman, M.S.A.,Furmanova-Hollenstein, P.,Pascual, G.,B van 't Wout, A.,Langedijk, J.P.M.,McLellan, J.S. Transient opening of trimeric prefusion RSV F proteins. Nat Commun, 10:2105-2105, 2019 Cited by PubMed Abstract: The respiratory syncytial virus (RSV) F glycoprotein is a class I fusion protein that mediates viral entry and is a major target of neutralizing antibodies. Structures of prefusion forms of RSV F, as well as other class I fusion proteins, have revealed compact trimeric arrangements, yet whether these trimeric forms can transiently open remains unknown. Here, we perform structural and biochemical studies on a recently isolated antibody, CR9501, and demonstrate that it enhances the opening of prefusion-stabilized RSV F trimers. The 3.3 Å crystal structure of monomeric RSV F bound to CR9501, combined with analysis of over 25 previously determined RSV F structures, reveals a breathing motion of the prefusion conformation. We also demonstrate that full-length RSV F trimers transiently open and dissociate on the cell surface. Collectively, these findings have implications for the function of class I fusion proteins, as well as antibody prophylaxis and vaccine development for RSV. PubMed: 31068578DOI: 10.1038/s41467-019-09807-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.1 Å) |
Structure validation
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