8G7V

Cryo-EM structure of Riplet:RIG-I:dsRNA complex (end-inter)

8G7V の概要

• エントリーDOI: 10.2210/pdb8g7v/pdb
• EMDBエントリー: 29825
• 分子名称: Antiviral innate immune response receptor RIG-I, E3 ubiquitin-protein ligase RNF135, p3dsRNA24a, ... (5 entities in total)
• 機能のキーワード: ribonucleoprotein complex, rna sensor, rig-i like receptor, ubiquitination, e3 ligase, trim family, antiviral protein, transferase-hydrolase-rna complex, transferase/hydrolase/rna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 325178.67

構造登録者

Wang, W.,Pyle, A.M. (登録日: 2023-02-17, 公開日: 2023-11-15, 最終更新日: 2025-05-28)

主引用文献

Wang, W.,Gotte, B.,Guo, R.,Pyle, A.M.
The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization.
Nat Commun, 14:7308-7308, 2023

PubMed Abstract: RIG-I is an essential innate immune receptor that responds to infection by RNA viruses. The RIG-I signaling cascade is mediated by a series of post-translational modifications, the most important of which is ubiquitination of the RIG-I Caspase Recruitment Domains (CARDs) by E3 ligase Riplet. This is required for interaction between RIG-I and its downstream adapter protein MAVS, but the mechanism of action remains unclear. Here we show that Riplet is required for RIG-I signaling in the presence of both short and long dsRNAs, establishing that Riplet activation does not depend upon RIG-I filament formation on long dsRNAs. Likewise, quantitative Riplet-RIG-I affinity measurements establish that Riplet interacts with RIG-I regardless of whether the receptor is bound to RNA. To understand this, we solved high-resolution cryo-EM structures of RIG-I/RNA/Riplet complexes, revealing molecular interfaces that control Riplet-mediated activation and enabling the formulation of a unified model for the role of Riplet in signaling.

PubMed: 37951994
DOI: 10.1038/s41467-023-42982-0

実験手法

ELECTRON MICROSCOPY (3.9 Å)