3HAG

Crystal structure of the Hepatitis E Virus-like Particle

3HAG の概要

• エントリーDOI: 10.2210/pdb3hag/pdb
• 分子名称: Capsid protein (1 entity in total)
• 機能のキーワード: jelly-roll beta sheets, beta barrel, virus, icosahedral virus
• 由来する生物種: Hepatitis E virus type 4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54446.56

構造登録者

Guu, T.S.Y.,Liu, Z.,Ye, Q.,Mata, D.A.,Li, K.,Yin, C.,Zhang, J.,Tao, Y.J. (登録日: 2009-05-01, 公開日: 2009-09-01, 最終更新日: 2024-04-03)

主引用文献

Guu, T.S.,Liu, Z.,Ye, Q.,Mata, D.A.,Li, K.,Yin, C.,Zhang, J.,Tao, Y.J.
Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding.
Proc.Natl.Acad.Sci.USA, 106:12992-12997, 2009

PubMed Abstract: Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-A structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt beta-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T = 3 capsid contains flat dimers, with less curvature than those of T = 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.

PubMed: 19622744
DOI: 10.1073/pnas.0904848106

実験手法

X-RAY DIFFRACTION (3.5 Å)