5lkc

Protruding domain of GII.17 norovirus Kawasaki308 in complex with HBGA type A (triglycan)

spinqualitylabelsall models 5lkc, resolution 1.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lkc is a 2 chain structure with sequence from Norovirus GII. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.81Å Ligands: A2G, EDO, FUC, GLA, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0E4B1P1_9CALI Publication Abstract from PubMed Human noroviruses are the leading cause of outbreaks of acute gastroenteritis. Norovirus interactions with histo-blood group antigens (HBGAs) are known to be important for an infection. In this study, we identified the HBGA binding pocket for an emerging GII genotype 17 (GII.17) variant using X-ray crystallography. The GII.17 variant bound the HBGA with an equivalent set of residues as the leading pandemic GII.4 variants. These structural data highlights the conserved nature of HBGA binding site between prevalent GII noroviruses. Noroviruses also interact with human milk oligosaccharides (HMOs), which mimic HBGAs and may function as receptor decoys. We previously showed that HMOs inhibited the binding of rarely detected GII.10 norovirus to HBGAs. We now found that an HMO, 2'-fucosyllactose (2'FL), additionally blocked both the GI.1 and GII.17 noroviruses from binding to HBGAs. Together, these findings provide evidence that 2'FL might function as a broadly reactive antiviral against multiple norovirus genogroups. Human norovirus inhibition by a human milk oligosaccharide.,Koromyslova A, Tripathi S, Morozov V, Schroten H, Hansman GS Virology. 2017 May 12;508:81-89. doi: 10.1016/j.virol.2017.04.032. PMID:28505592 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

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