8UFB
Eastern equine encephalitis virus (PE-6) VLP in complex with full-length VLDLR (asymmetric unit)
This is a non-PDB format compatible entry.
Summary for 8UFB
| Entry DOI | 10.2210/pdb8ufb/pdb |
| EMDB information | 42190 |
| Descriptor | E1 protein, E2 protein, Capsid protein, ... (6 entities in total) |
| Functional Keywords | virus, receptor, structural genomics, center for structural biology of infectious diseases, csbid, viral protein |
| Biological source | Eastern equine encephalitis virus More |
| Total number of polymer chains | 20 |
| Total formula weight | 1109662.71 |
| Authors | Adams, L.J.,Fremont, D.H.,Center for Structural Biology of Infectious Diseases (CSBID) (deposition date: 2023-10-04, release date: 2024-01-17, Last modification date: 2024-10-23) |
| Primary citation | Adams, L.J.,Raju, S.,Ma, H.,Gilliland Jr., T.,Reed, D.S.,Klimstra, W.B.,Fremont, D.H.,Diamond, M.S. Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus. Cell, 187:360-374.e19, 2024 Cited by PubMed Abstract: The very-low-density lipoprotein receptor (VLDLR) comprises eight LDLR type A (LA) domains and supports entry of distantly related alphaviruses, including Eastern equine encephalitis virus (EEEV) and Semliki Forest virus (SFV). Here, by resolving multiple cryo-electron microscopy structures of EEEV-VLDLR complexes and performing mutagenesis and functional studies, we show that EEEV uses multiple sites (E1/E2 cleft and E2 A domain) to engage more than one LA domain simultaneously. However, no single LA domain is necessary or sufficient to support efficient EEEV infection. Whereas all EEEV strains show conservation of two VLDLR-binding sites, the EEEV PE-6 strain and a few other EEE complex members feature a single amino acid substitution that enables binding of LA domains to an additional site on the E2 B domain. These structural and functional analyses informed the design of a minimal VLDLR decoy receptor that neutralizes EEEV infection and protects mice from lethal challenge. PubMed: 38176410DOI: 10.1016/j.cell.2023.11.031 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.89 Å) |
Structure validation
Download full validation report
