8ufb | pdb_00008ufb

Eastern equine encephalitis virus (PE-6) VLP in complex with full-length VLDLR (asymmetric unit)

spinqualitylabelsall models 8ufb, resolution 3.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ufb is a 20 chain structure with sequence from Eastern equine encephalitis virus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.89Å Ligands: CA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q88678_EEEV Publication Abstract from PubMed 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. Structural and functional basis of VLDLR usage by Eastern equine encephalitis virus.,Adams LJ, Raju S, Ma H, Gilliland T Jr, Reed DS, Klimstra WB, Fremont DH, Diamond MS Cell. 2024 Jan 18;187(2):360-374.e19. doi: 10.1016/j.cell.2023.11.031. Epub 2024 , Jan 3. PMID:38176410 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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