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3PHF

Crystal Structure of the Epstein-Barr virus gH and gL complex

3PHF の概要
エントリーDOI10.2210/pdb3phf/pdb
関連するPDBエントリー3M1C
分子名称Envelope glycoprotein H, Envelope glycoprotein L (2 entities in total)
機能のキーワードvirus entry, membrane fusion, glycoprotein, viral protein
由来する生物種Human herpesvirus 4 (Epstein-Barr virus)
詳細
細胞内の位置Virion membrane; Single-pass membrane protein (Potential): P03231
Virion membrane; Peripheral membrane protein; Extracellular side (By similarity): P03212
タンパク質・核酸の鎖数32
化学式量合計1347944.26
構造登録者
Matsuura, H.,Kirschner, A.N.,Jardetzky, T.S. (登録日: 2010-11-04, 公開日: 2011-01-12, 最終更新日: 2024-11-27)
主引用文献Matsuura, H.,Kirschner, A.N.,Longnecker, R.,Jardetzky, T.S.
Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex.
Proc.Natl.Acad.Sci.USA, 107:22641-22646, 2010
Cited by
PubMed Abstract: The Epstein-Barr virus (EBV) is a γ-herpesvirus that infects B cells and epithelial cells and that has been linked to malignancies in both cell types in vivo. EBV, like other herpesviruses, has three glycoproteins, glycoprotein B (gB), gH, and gL, that form the core membrane fusion machinery mediating viral penetration into the cell. The gH and gL proteins associate to form a heterodimeric complex, which is necessary for efficient membrane fusion and also implicated in direct binding to epithelial cell receptors required for viral entry. To gain insight into the mechanistic role of gH/gL, we determined the crystal structure of the EBV gH/gL complex. The structure is comprised of four domains organized along the longest axis of the molecule. Comparisons with homologous HSV-2 gH/gL and partial pseudorabies virus gH structures support the domain boundaries determined for the EBV gH/gL structure and illustrate significant differences in interdomain packing angles. The gL subunit and N-terminal residues of gH form a globular domain at one end of the structure, implicated in interactions with gB and activation of membrane fusion. The C-terminal domain of gH, proximal to the viral membrane, is also implicated in membrane fusion. The gH/gL structure locates an integrin binding motif, implicated in epithelial cell entry, on a prominent loop in the central region of the structure. Multiple regions of gH/gL, including its two extreme ends, are functionally important, consistent with the multiple roles of gH/gL in EBV entry.
PubMed: 21149717
DOI: 10.1073/pnas.1011806108
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.58 Å)
構造検証レポート
Validation report summary of 3phf
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-25に公開中

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