5e65 | pdb_00005e65

The complex structure of Hemagglutinin-esterase-fusion mutant protein from the influenza D virus with receptor analog 9-O-Ac-3'SLN (Tr322)

spinqualitylabelsall models 5e65, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e65 is a 4 chain structure with sequence from Influenza D virus (D/swine/Oklahoma/1334/2011). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: 5N6, BMA, GAL, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K9LG83_9ORTO Publication Abstract from PubMed Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health. An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.,Song H, Qi J, Khedri Z, Diaz S, Yu H, Chen X, Varki A, Shi Y, Gao GF PLoS Pathog. 2016 Jan 27;12(1):e1005411. doi: 10.1371/journal.ppat.1005411., eCollection 2016 Jan. PMID:26816272 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemagglutinin-esterase 3D structures

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