4qy2 | pdb_00004qy2

Structure of H10 from human-infecting H10N8 virus in complex with human receptor analog

spinqualitylabelsall models 4qy2, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qy2 is a 12 chain structure with sequence from Influenza A virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.399Å Ligands: NAG, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A059T4A1_9INFA Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324][SAAS:SAAS00046810] Publication Abstract from PubMed Since December 2013, at least three cases of human infections with H10N8 avian influenza virus have been reported in China, two of them being fatal. To investigate the epidemic potential of H10N8 viruses, we examined the receptor binding property of the first human isolate, A/Jiangxi-Donghu/346/2013 (JD-H10N8), and determined the structures of its haemagglutinin (HA) in complex with both avian and human receptor analogues. Our results suggest that JD-H10N8 preferentially binds the avian receptor and that residue R137-localized within the receptor-binding site of HA-plays a key role in this preferential binding. Compared with the H7N9 avian influenza viruses, JD-H10N8 did not exhibit the enhanced binding to human receptors observed with the prevalent H7N9 virus isolate Anhui-1, but resembled the receptor binding activity of the early-outbreak H7N9 isolate (Shanghai-1). We conclude that the H10N8 virus is a typical avian influenza virus. Structural basis for preferential avian receptor binding by the human-infecting H10N8 avian influenza virus.,Wang M, Zhang W, Qi J, Wang F, Zhou J, Bi Y, Wu Y, Sun H, Liu J, Huang C, Li X, Yan J, Shu Y, Shi Y, Gao GF Nat Commun. 2015 Jan 9;6:5600. doi: 10.1038/ncomms6600. PMID:25574798 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemagglutinin 3D structures

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