3MX5

Lassa fever virus nucleoprotein complexed with UTP

3MX5 の概要

• エントリーDOI: 10.2210/pdb3mx5/pdb
• 関連するPDBエントリー: 3MWP 3MWT 3MX2
• 分子名称: Nucleoprotein, URIDINE 5'-TRIPHOSPHATE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: nucleoprotein, lassa fever virus, structural genomics, scottish structural proteomics facility, sspf, nuclear protein
• 由来する生物種: Lassa virus (LASV)
• 細胞内の位置: Virion: P13699
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 193544.09

構造登録者

Qi, X.,Lan, S.,Wang, W.,Schelde, L.M.,Dong, H.,Wallat, G.,Liang, Y.,Ly, H.,Dong, C.,Scottish Structural Proteomics Facility (SSPF) (登録日: 2010-05-06, 公開日: 2010-12-01, 最終更新日: 2023-09-06)

主引用文献

Qi, X.,Lan, S.,Wang, W.,Schelde, L.M.,Dong, H.,Wallat, G.D.,Ly, H.,Liang, Y.,Dong, C.
Cap binding and immune evasion revealed by Lassa nucleoprotein structure.
Nature, 468:779-783, 2010

PubMed Abstract: Lassa virus, the causative agent of Lassa fever, causes thousands of deaths annually and is a biological threat agent, for which there is no vaccine and limited therapy. The nucleoprotein (NP) of Lassa virus has essential roles in viral RNA synthesis and immune suppression, the molecular mechanisms of which are poorly understood. Here we report the crystal structure of Lassa virus NP at 1.80 Å resolution, which reveals amino (N)- and carboxy (C)-terminal domains with structures unlike any of the reported viral NPs. The N domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription, whereas the C domain contains 3'-5' exoribonuclease activity involved in suppressing interferon induction. To our knowledge this is the first X-ray crystal structure solved for an arenaviral NP, which reveals its unexpected functions and indicates unique mechanisms in cap binding and immune evasion. These findings provide great potential for vaccine and drug development.

PubMed: 21085117
DOI: 10.1038/nature09605

実験手法

X-RAY DIFFRACTION (1.903 Å)