4ild

Crystal structure of truncated Bovine viral diarrhea virus 1 E2 envelope protein

spinqualitylabelsall models 4ild, resolution 3.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ild is a 2 chain structure with sequence from Bovine viral diarrhea virus 1-NADL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.27Å Ligands: CA, IUM, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function POLG_BVDVN Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (Probable). P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity). Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity (By similarity). RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome. Publication Abstract from PubMed Pestiviruses, including bovine viral diarrhea virus, are important animal pathogens and are closely related to hepatitis C virus, which remains a major global health threat. They have an outer lipid envelope bearing two glycoproteins, E1 and E2, required for cell entry. They deliver their genome into the host cell cytoplasm by fusion of their envelope with a cellular membrane. The crystal structure of bovine viral diarrhea virus E2 reveals a unique protein architecture consisting of two Ig-like domains followed by an elongated beta-stranded domain with a new fold. E2 forms end-to-end homodimers with a conserved C-terminal motif rich in aromatic residues at the contact. A disulfide bond across the interface explains the acid resistance of pestiviruses and their requirement for a redox activation step to initiate fusion. From the structure of E2, we propose alternative possible membrane fusion mechanisms. We expect the pestivirus fusion apparatus to be conserved in hepatitis C virus. Crystal structure of glycoprotein E2 from bovine viral diarrhea virus.,Li Y, Wang J, Kanai R, Modis Y Proc Natl Acad Sci U S A. 2013 Apr 8. PMID:23569276 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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