6H9V

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

6H9V の概要

• エントリーDOI: 10.2210/pdb6h9v/pdb
• 関連するPDBエントリー: 4OO6
• 分子名称: VP1, methyl alpha-L-fucopyranoside, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: viral capsid protein, protruding domain, viral protein, isoaspartate, isopeptide, fucose, glycan, receptor
• 由来する生物種: Norovirus Hu/GII-4/Saga4/2006/JP
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68489.07

構造登録者

Meyer, P.H.O.,Blaum, B.S. (登録日: 2018-08-06, 公開日: 2019-04-03, 最終更新日: 2024-11-13)

主引用文献

Mallagaray, A.,Creutznacher, R.,Dulfer, J.,Mayer, P.H.O.,Grimm, L.L.,Orduna, J.M.,Trabjerg, E.,Stehle, T.,Rand, K.D.,Blaum, B.S.,Uetrecht, C.,Peters, T.
A post-translational modification of human Norovirus capsid protein attenuates glycan binding.
Nat Commun, 10:1320-1320, 2019

PubMed Abstract: 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.

PubMed: 30899001
DOI: 10.1038/s41467-019-09251-5

実験手法

X-RAY DIFFRACTION (1.52 Å)