8IHP

Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3

これはPDB形式変換不可エントリーです。

8IHP の概要

• エントリーDOI: 10.2210/pdb8ihp/pdb
• EMDBエントリー: 35451
• 分子名称: Spike glycoprotein E2, Spike glycoprotein E1, Capsid protein, ... (6 entities in total)
• 機能のキーワード: semliki forest virus, sfv, receptor, complex, vldlr, glycoprotein, viral protein
• 由来する生物種: Semliki Forest virus (SFV); 詳細
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 464693.35

構造登録者

Cao, D.,Ma, B.,Cao, Z.,Zhang, X.,Xiang, Y. (登録日: 2023-02-23, 公開日: 2023-04-12, 最終更新日: 2025-07-02)

主引用文献

Cao, D.,Ma, B.,Cao, Z.,Zhang, X.,Xiang, Y.
Structure of Semliki Forest virus in complex with its receptor VLDLR.
Cell, 186:2208-2218.e15, 2023

PubMed Abstract: Semliki Forest virus (SFV) is an alphavirus that uses the very-low-density lipoprotein receptor (VLDLR) as a receptor during infection of its vertebrate hosts and insect vectors. Herein, we used cryoelectron microscopy to study the structure of SFV in complex with VLDLR. We found that VLDLR binds multiple E1-DIII sites of SFV through its membrane-distal LDLR class A (LA) repeats. Among the LA repeats of the VLDLR, LA3 has the best binding affinity to SFV. The high-resolution structure shows that LA3 binds SFV E1-DIII through a small surface area of 378 Å, with the main interactions at the interface involving salt bridges. Compared with the binding of single LA3s, consecutive LA repeats around LA3 promote synergistic binding to SFV, during which the LAs undergo a rotation, allowing simultaneous key interactions at multiple E1-DIII sites on the virion and enabling the binding of VLDLRs from divergent host species to SFV.

PubMed: 37098345
DOI: 10.1016/j.cell.2023.03.032

実験手法

ELECTRON MICROSCOPY (3 Å)