6h9v | pdb_00006h9v

Crystal structure of deaminated P domain from norovirus strain Saga GII-4 in complex with Fuc

spinqualitylabelsall models 6h9v, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h9v is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MFU, MG NonStd Res: IAS Related: 4oo6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains. A post-translational modification of human Norovirus capsid protein attenuates glycan binding.,Mallagaray A, Creutznacher R, Dulfer J, Mayer PHO, Grimm LL, Orduna JM, Trabjerg E, Stehle T, Rand KD, Blaum BS, Uetrecht C, Peters T Nat Commun. 2019 Mar 21;10(1):1320. doi: 10.1038/s41467-019-09251-5. PMID:30899001 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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