2OBR

Crystal Structures of P Domain of Norovirus VA387

2OBR の概要

• エントリーDOI: 10.2210/pdb2obr/pdb
• 分子名称: Capsid protein (2 entities in total)
• 機能のキーワード: crystal structures, p domain, norovirus va387, viral protein
• 由来する生物種: Norovirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35982.21

構造登録者

Cao, S.,Lou, Z.,Jiang, X.,Zhang, X.C.,Li, X.,Rao, Z. (登録日: 2006-12-20, 公開日: 2007-04-24, 最終更新日: 2023-10-25)

主引用文献

Cao, S.,Lou, Z.,Tan, M.,Chen, Y.,Liu, Y.,Zhang, Z.,Zhang, X.C.,Jiang, X.,Li, X.,Rao, Z.
Structural basis for the recognition of blood group trisaccharides by norovirus.
J.Virol., 81:5949-5957, 2007

PubMed Abstract: Noroviruses are one of the major causes of nonbacterial gastroenteritis epidemics in humans. Recent studies on norovirus receptors show that different noroviruses recognize different human histo-blood group antigens (HBGAs), and eight receptor binding patterns of noroviruses have been identified. The P domain of the norovirus capsids is directly involved in this recognition. To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus, VA387, was cocrystallized with synthetic type A or B trisaccharides. Based on complex crystal structures observed at a 2.0-A resolution, we demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand. The A and B trisaccharides display similar binding modes, and the common fucose ring plays a key role in this interaction. The extensive interface between the two protomers in a P dimer also plays a crucial role in the formation of the receptor binding interface.

PubMed: 17392366
DOI: 10.1128/JVI.00219-07

実験手法

X-RAY DIFFRACTION (2.2 Å)