4RPB

Crystal Structure of P Domain of Snow Mountain Norovirus

4RPB の概要

• エントリーDOI: 10.2210/pdb4rpb/pdb
• 分子名称: Capsid protein VP1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: virus internalization, hbga, virus surface, viral protein
• 由来する生物種: NOROVIRUS HU/GII.2/KL109/1978/MYS
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 102467.81

構造登録者

Singh, B.K.,Hansman, G.S. (登録日: 2014-10-30, 公開日: 2016-06-22, 最終更新日: 2024-02-28)

主引用文献

Singh, B.K.,Leuthold, M.M.,Hansman, G.S.
Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens.
Msphere, 1:-, 2016

PubMed Abstract: Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Most human noroviruses bind HBGAs, while some strains were found to have minimal or no HBGA interactions. Here, we explain some possible structural constraints for several noroviruses that were found to bind poorly to HBGAs by using X-ray crystallography. We showed that one aspartic acid was flexible or positioned away from the fucose moiety of the HBGAs and this likely hindered binding, although other fucose-interacting residues were perfectly oriented. Interestingly, a neighboring loop also appeared to influence the loop hosting the aspartic acid. These new findings might explain why some human noroviruses bound HBGAs poorly, although further studies are required.

PubMed: 27303720
DOI: 10.1128/mSphere.00049-16

実験手法

X-RAY DIFFRACTION (1.61 Å)