2I69

Crystal structure of the West Nile virus envelope glycoprotein

2I69 の概要

• エントリーDOI: 10.2210/pdb2i69/pdb
• 分子名称: Polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: viral membrane fusion protein, receptor binding, antibody epitope, igc, beta sandwich, glycoprotein, viral protein
• 由来する生物種: West Nile virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44073.85

構造登録者

Kanai, R.,Modis, Y. (登録日: 2006-08-28, 公開日: 2006-11-21, 最終更新日: 2024-10-30)

主引用文献

Kanai, R.,Kar, K.,Anthony, K.,Gould, L.H.,Ledizet, M.,Fikrig, E.,Marasco, W.A.,Koski, R.A.,Modis, Y.
Crystal structure of west nile virus envelope glycoprotein reveals viral surface epitopes.
J.Virol., 80:11000-11008, 2006

PubMed Abstract: West Nile virus, a member of the Flavivirus genus, causes fever that can progress to life-threatening encephalitis. The major envelope glycoprotein, E, of these viruses mediates viral attachment and entry by membrane fusion. We have determined the crystal structure of a soluble fragment of West Nile virus E. The structure adopts the same overall fold as that of the E proteins from dengue and tick-borne encephalitis viruses. The conformation of domain II is different from that in other prefusion E structures, however, and resembles the conformation of domain II in postfusion E structures. The epitopes of neutralizing West Nile virus-specific antibodies map to a region of domain III that is exposed on the viral surface and has been implicated in receptor binding. In contrast, we show that certain recombinant therapeutic antibodies, which cross-neutralize West Nile and dengue viruses, bind a peptide from domain I that is exposed only during the membrane fusion transition. By revealing the details of the molecular landscape of the West Nile virus surface, our structure will assist the design of antiviral vaccines and therapeutics.

PubMed: 16943291
DOI: 10.1128/JVI.01735-06

実験手法

X-RAY DIFFRACTION (3.11 Å)