3FVC

Crystal structure of a trimeric variant of the Epstein-Barr virus glycoprotein B

3FVC の概要

• エントリーDOI: 10.2210/pdb3fvc/pdb
• 分子名称: Glycoprotein GP110, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: viral fusion protein, ph domains, fusion loops, glycoprotein, late protein, membrane, transmembrane, viral protein
• 由来する生物種: Human herpesvirus 4
• 細胞内の位置: Virion membrane ; Single-pass type I membrane protein : P03188
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 75266.05

構造登録者

Backovic, M. (登録日: 2009-01-15, 公開日: 2009-03-17, 最終更新日: 2024-10-30)

主引用文献

Backovic, M.,Longnecker, R.,Jardetzky, T.S.
Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
Proc.Natl.Acad.Sci.USA, 106:2880-2885, 2009

PubMed Abstract: Epstein-Barr virus (EBV) is a herpesvirus that is associated with development of malignancies of lymphoid tissue. EBV infections are life-long and occur in >90% of the population. Herpesviruses enter host cells in a process that involves fusion of viral and cellular membranes. The fusion apparatus is comprised of envelope glycoprotein B (gB) and a heterodimeric complex made of glycoproteins H and L. Glycoprotein B is the most conserved envelope glycoprotein in human herpesviruses, and the structure of gB from Herpes simplex virus 1 (HSV-1) is available. Here, we report the crystal structure of the secreted EBV gB ectodomain, which forms 16-nm long spike-like trimers, structurally homologous to the postfusion trimers of the fusion protein G of vesicular stomatitis virus (VSV). Comparative structural analyses of EBV gB and VSV G, which has been solved in its pre and postfusion states, shed light on gB residues that may be involved in conformational changes and membrane fusion. Also, the EBV gB structure reveals that, despite the high sequence conservation of gB in herpesviruses, the relative orientations of individual domains, the surface charge distributions, and the structural details of EBV gB differ from the HSV-1 protein, indicating regions and residues that may have important roles in virus-specific entry.

PubMed: 19196955
DOI: 10.1073/pnas.0810530106

実験手法

X-RAY DIFFRACTION (3.2 Å)