7N1H

CryoEM structure of Venezuelan equine encephalitis virus VLP in complex with the LDLRAD3 receptor

これはPDB形式変換不可エントリーです。

7N1H の概要

• エントリーDOI: 10.2210/pdb7n1h/pdb
• EMDBエントリー: 24116 24394
• 分子名称: Low-density lipoprotein receptor class A domain-containing protein 3, E1 envelope glycoprotein, E2 envelope glycoprotein, ... (6 entities in total)
• 機能のキーワード: veev, viral envelope, host receptor, low-density lipoprotein receptor type-a module, ldlrad3, encephalitic alphavirus, structural genomics, center for structural genomics of infectious diseases, csgid, virus like particle
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 472228.03

構造登録者

Basore, K.,Nelson, C.A.,Fremont, D.H.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2021-05-27, 公開日: 2021-10-13, 最終更新日: 2024-11-20)

主引用文献

Basore, K.,Ma, H.,Kafai, N.M.,Mackin, S.,Kim, A.S.,Nelson, C.A.,Diamond, M.S.,Fremont, D.H.
Structure of Venezuelan equine encephalitis virus in complex with the LDLRAD3 receptor.
Nature, 598:672-676, 2021

PubMed Abstract: LDLRAD3 is a recently defined attachment and entry receptor for Venezuelan equine encephalitis virus (VEEV), a New World alphavirus that causes severe neurological disease in humans. Here we present near-atomic-resolution cryo-electron microscopy reconstructions of VEEV virus-like particles alone and in a complex with the ectodomains of LDLRAD3. Domain 1 of LDLRAD3 is a low-density lipoprotein receptor type-A module that binds to VEEV by wedging into a cleft created by two adjacent E2-E1 heterodimers in one trimeric spike, and engages domains A and B of E2 and the fusion loop in E1. Atomic modelling of this interface is supported by mutagenesis and anti-VEEV antibody binding competition assays. Notably, VEEV engages LDLRAD3 in a manner that is similar to the way that arthritogenic alphaviruses bind to the structurally unrelated MXRA8 receptor, but with a much smaller interface. These studies further elucidate the structural basis of alphavirus-receptor interactions, which could inform the development of therapies to mitigate infection and disease against multiple members of this family.

PubMed: 34646020
DOI: 10.1038/s41586-021-03963-9

実験手法

ELECTRON MICROSCOPY (4.3 Å)