8pag

Crystal structure of the ectodomain of Norway rat pestivirus E2 glycoprotein

spinqualitylabelsall models 8pag, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8pag is a 1 chain structure with sequence from Norway rat pestivirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: BMA, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Pestiviruses, within the family Flaviviridae, are economically important viruses of livestock. In recent years, new pestiviruses have been reported in domestic animals and non-cloven-hoofed animals. Among them, atypical porcine pestivirus (APPV) and Norway rat pestivirus (NRPV) have relatively little sequence conservation in their surface glycoprotein E2. Despite E2 being the main target for neutralizing antibodies and necessary for cell attachment and viral fusion, the mechanism of viral entry remains elusive. To gain further insights into the pestivirus E2 mechanism of action and to assess its diversity within the genus, we report X-ray structures of the pestivirus E2 proteins from APPV and NRPV. Despite the highly divergent structures, both are able to dimerize through their C-terminal domain and contain a solvent-exposed beta-hairpin reported to be involved in host receptor binding. Functional analysis of this beta-hairpin in the context of BVDV revealed its ability to rescue viral infectivity. Structural comparison of typical and atypical E2 pestivirus glycoproteins.,Aitkenhead H, Riedel C, Cowieson N, Rumenapf HT, Stuart DI, El Omari K Structure. 2024 Mar 7;32(3):273-281.e4. doi: 10.1016/j.str.2023.12.003. Epub 2024 , Jan 3. PMID:38176409 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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