7FFE

Cryo-EM structure of VEEV VLP

これはPDB形式変換不可エントリーです。

7FFE の概要

• エントリーDOI: 10.2210/pdb7ffe/pdb
• EMDBエントリー: 31566
• 分子名称: Capsid protein, Spike glycoprotein E1, assembly protein E3, ... (4 entities in total)
• 機能のキーワード: virus, receptor, complex, virus like particle
• 由来する生物種: Venezuelan equine encephalitis virus (strain TC-83) (VEEV); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 530140.86

構造登録者

Zhang, X.,Xiang, Y.,Ma, J.,Ma, B.,Huang, C. (登録日: 2021-07-23, 公開日: 2021-10-20, 最終更新日: 2024-10-16)

主引用文献

Ma, B.,Huang, C.,Ma, J.,Xiang, Y.,Zhang, X.
Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3.
Nature, 598:677-681, 2021

PubMed Abstract: Venezuelan equine encephalitis virus (VEEV) is an enveloped RNA virus that causes encephalitis and potentially mortality in infected humans and equines. At present, no vaccines or drugs are available that prevent or cure diseases caused by VEEV. Low-density lipoprotein receptor class A domain-containing 3 (LDLRAD3) was recently identified as a receptor for the entry of VEEV into host cells. Here we present the cryo-electron microscopy structure of the LDLRAD3 extracellular domain 1 (LDLRAD3-D1) in complex with VEEV virus-like particles at a resolution of 3.0 Å. LDLRAD3-D1 has a cork-like structure and is inserted into clefts formed between adjacent VEEV E2-E1 heterodimers in the viral-surface trimer spikes through hydrophobic and polar contacts. Mutagenesis studies of LDLRAD3-D1 identified residues that are involved in the key interactions with VEEV. Of note, some of the LDLRAD3-D1 mutants showed a significantly increased binding affinity for VEEV, suggesting that LDLRAD3-D1 may serve as a potential scaffold for the development of inhibitors of VEEV entry. Our structures provide insights into alphavirus assembly and the binding of receptors to alphaviruses, which may guide the development of therapeutic countermeasures against alphaviruses.

PubMed: 34646021
DOI: 10.1038/s41586-021-03909-1

実験手法

ELECTRON MICROSCOPY (3.5 Å)