3G7T

Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation

3G7T の概要

• エントリーDOI: 10.2210/pdb3g7t/pdb
• 分子名称: Envelope protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: membrane fusion protein, envelope protein, membrane anchor, fusion loop, igc domain, beta sandwich, glycoprotein, membrane, transmembrane, virion, viral protein
• 由来する生物種: Dengue virus 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43786.34

構造登録者

Modis, Y. (登録日: 2009-02-10, 公開日: 2009-04-21, 最終更新日: 2024-11-20)

主引用文献

Nayak, V.,Dessau, M.,Kucera, K.,Anthony, K.,Ledizet, M.,Modis, Y.
Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion.
J.Virol., 83:4338-4344, 2009

PubMed Abstract: Dengue virus relies on a conformational change in its envelope protein, E, to fuse the viral lipid membrane with the endosomal membrane and thereby deliver the viral genome into the cytosol. We have determined the crystal structure of a soluble fragment E (sE) of dengue virus type 1 (DEN-1). The protein is in the postfusion conformation even though it was not exposed to a lipid membrane or detergent. At the domain I-domain III interface, 4 polar residues form a tight cluster that is absent in other flaviviral postfusion structures. Two of these residues, His-282 and His-317, are conserved in flaviviruses and are part of the "pH sensor" that triggers the fusogenic conformational change in E, at the reduced pH of the endosome. In the fusion loop, Phe-108 adopts a distinct conformation, forming additional trimer contacts and filling the bowl-shaped concavity observed at the tip of the DEN-2 sE trimer.

PubMed: 19244332
DOI: 10.1128/JVI.02574-08

実験手法

X-RAY DIFFRACTION (3.5 Å)