3FD4

Crystal Structure of Epstein-Barr virus gp42 protein

3FD4 の概要

• エントリーDOI: 10.2210/pdb3fd4/pdb
• 分子名称: Glycoprotein gp42 (2 entities in total)
• 機能のキーワード: c type lectin, herpesvirus, virus entry, membrane fusion, host-virus interaction, lectin, membrane, transmembrane, viral protein
• 由来する生物種: Human herpesvirus 4 (strain B95-8)
• 細胞内の位置: Virion membrane : P03205
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43252.99

構造登録者

Kirschner, A.,Jardetzky, T. (登録日: 2008-11-24, 公開日: 2009-06-23, 最終更新日: 2024-10-30)

主引用文献

Kirschner, A.N.,Sorem, J.,Longnecker, R.,Jardetzky, T.S.
Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry.
Structure, 17:223-233, 2009

PubMed Abstract: Epstein-Barr virus requires glycoproteins gH/gL, gB, and gp42 to fuse its lipid envelope with B cells. Gp42 is a type II membrane protein consisting of a flexible N-terminal region, which binds gH/gL, and a C-terminal lectin-like domain that binds to the B-cell entry receptor human leukocyte antigen (HLA) class II. Gp42 triggers membrane fusion after HLA binding, a process that requires simultaneous binding to gH/gL and a functional hydrophobic pocket in the lectin domain adjacent to the HLA binding site. Here we present the structure of gp42 in its unbound form. Comparisons to the previously determined structure of a gp42:HLA complex reveals additional N-terminal residues forming part of the gH/gL binding site and structural changes in the receptor binding domain. Although the core of the lectin domain remains similar, significant shifts in two loops and an alpha helix bordering the essential hydrophobic pocket suggest a structural mechanism for triggering fusion.

PubMed: 19217393
DOI: 10.1016/j.str.2008.12.010

実験手法

X-RAY DIFFRACTION (2.4 Å)