3N41

Crystal structure of the mature envelope glycoprotein complex (spontaneous cleavage) of Chikungunya virus.

3N41 の概要

• エントリーDOI: 10.2210/pdb3n41/pdb
• 関連するPDBエントリー: 1RER 2ALA 3MUU 3MUW
• EMDBエントリー: 1015 1121
• 分子名称: E3 envelope glycoprotein, E2 envelope glycoprotein, E1 envelope glycoprotein, ... (6 entities in total)
• 機能のキーワード: viral protein, immature heterodimer, alphavirus, receptor binding, membrane fusion
• 由来する生物種: Chikungunya virus (CHIKV); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 99073.35

構造登録者

Voss, J.,Vaney, M.C.,Duquerroy, S.,Rey, F.A. (登録日: 2010-05-21, 公開日: 2010-12-01, 最終更新日: 2024-11-20)

主引用文献

Voss, J.E.,Vaney, M.C.,Duquerroy, S.,Vonrhein, C.,Girard-Blanc, C.,Crublet, E.,Thompson, A.,Bricogne, G.,Rey, F.A.
Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography.
Nature, 468:709-712, 2010

PubMed Abstract: Chikungunya virus (CHIKV) is an emerging mosquito-borne alphavirus that has caused widespread outbreaks of debilitating human disease in the past five years. CHIKV invasion of susceptible cells is mediated by two viral glycoproteins, E1 and E2, which carry the main antigenic determinants and form an icosahedral shell at the virion surface. Glycoprotein E2, derived from furin cleavage of the p62 precursor into E3 and E2, is responsible for receptor binding, and E1 for membrane fusion. In the context of a concerted multidisciplinary effort to understand the biology of CHIKV, here we report the crystal structures of the precursor p62-E1 heterodimer and of the mature E3-E2-E1 glycoprotein complexes. The resulting atomic models allow the synthesis of a wealth of genetic, biochemical, immunological and electron microscopy data accumulated over the years on alphaviruses in general. This combination yields a detailed picture of the functional architecture of the 25 MDa alphavirus surface glycoprotein shell. Together with the accompanying report on the structure of the Sindbis virus E2-E1 heterodimer at acidic pH (ref. 3), this work also provides new insight into the acid-triggered conformational change on the virus particle and its inbuilt inhibition mechanism in the immature complex.

PubMed: 21124458
DOI: 10.1038/nature09555

実験手法

X-RAY DIFFRACTION (3.01 Å)