6SNB

Structure of Coxsackievirus A10 A-particle

6SNB の概要

• エントリーDOI: 10.2210/pdb6snb/pdb
• 関連するPDBエントリー: 6SMG
• EMDBエントリー: 10256
• 分子名称: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3 (3 entities in total)
• 機能のキーワード: cv-a10, kremen1, virus-receptor complex, hand, foot and mouth disease, virus, picornavirus uncoating intermediate
• 由来する生物種: Coxsackievirus A10; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87141.07

構造登録者

Zhao, Y.,Zhou, D.,Ni, T.,Karia, D.,Kotecha, A.,Wang, X.,Rao, Z.,Jones, E.Y.,Fry, E.E.,Ren, J.,Stuart, D.I. (登録日: 2019-08-23, 公開日: 2020-01-15, 最終更新日: 2025-07-02)

主引用文献

Zhao, Y.,Zhou, D.,Ni, T.,Karia, D.,Kotecha, A.,Wang, X.,Rao, Z.,Jones, E.Y.,Fry, E.E.,Ren, J.,Stuart, D.I.
Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10.
Nat Commun, 11:38-38, 2020

PubMed Abstract: Coxsackievirus A10 (CV-A10) is responsible for an escalating number of severe infections in children, but no prophylactics or therapeutics are currently available. KREMEN1 (KRM1) is the entry receptor for the largest receptor-group of hand-foot-and-mouth disease causing viruses, which includes CV-A10. We report here structures of CV-A10 mature virus alone and in complex with KRM1 as well as of the CV-A10 A-particle. The receptor spans the viral canyon with a large footprint on the virus surface. The footprint has some overlap with that seen for the neonatal Fc receptor complexed with enterovirus E6 but is larger and distinct from that of another enterovirus receptor SCARB2. Reduced occupancy of a particle-stabilising pocket factor in the complexed virus and the presence of both unbound and expanded virus particles suggests receptor binding initiates a cascade of conformational changes that produces expanded particles primed for viral uncoating.

PubMed: 31911601
DOI: 10.1038/s41467-019-13936-2

実験手法

ELECTRON MICROSCOPY (4.4 Å)