6T40

Bovine enterovirus F3 in complex with a Cysteinylglycine dipeptide

6T40 の概要

• エントリーDOI: 10.2210/pdb6t40/pdb
• 分子名称: VP1, CYSTEINE, CHLORIDE ION, ... (12 entities in total)
• 機能のキーワード: enterovirus f3, enterovirus capsid assembly, glutathione, cys-gly dipeptide, virus
• 由来する生物種: Enterovirus F; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93329.63

構造登録者

Duyvesteyn, H.M.E.,Ren, J.,Walter, T.S.,Fry, E.E.,Stuart, D.I. (登録日: 2019-10-11, 公開日: 2020-08-19, 最終更新日: 2024-02-07)

主引用文献

Duyvesteyn, H.M.E.,Ren, J.,Walter, T.S.,Fry, E.E.,Stuart, D.I.
Glutathione facilitates enterovirus assembly by binding at a druggable pocket.
Commun Biol, 3:9-9, 2020

PubMed Abstract: Enteroviruses cause a range of human and animal diseases, some life-threatening, but there remain no licenced anti-enterovirus drugs. However, a benzene-sulfonamide derivative and related compounds have been shown recently to block infection of a range of enteroviruses by binding the capsid at a positively-charged surface depression conserved across many enteroviruses. It has also been established that glutathione is essential for the assembly of many enteroviruses, interacting with the capsid proteins to facilitate the formation of the pentameric assembly intermediate, although the mechanism is unknown. Here we show, by high resolution structure analyses of enterovirus F3, that reduced glutathione binds to the same interprotomer pocket as the benzene-sulfonamide derivative. Bound glutathione makes strong interactions with adjacent protomers, thereby explaining the underlying biological role of this druggable binding pocket and delineating the pharmacophore for potential antivirals.

PubMed: 31909201
DOI: 10.1038/s42003-019-0722-x

実験手法

X-RAY DIFFRACTION (1.67 Å)