4A2Q

Structure of duck RIG-I tandem CARDs and helicase domain

4A2Q の概要

• エントリーDOI: 10.2210/pdb4a2q/pdb
• 関連するPDBエントリー: 4A2P 4A2V 4A2W 4A2X 4A36
• 分子名称: RETINOIC ACID INDUCIBLE PROTEIN I (1 entity in total)
• 機能のキーワード: hydrolase, superfamily 2 rna helicase, atp and dsrna binding, antiviral signalling pathway
• 由来する生物種: ANAS PLATYRHYNCHOS
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 362933.38

構造登録者

Kowalinski, E.,Lunardi, T.,McCarthy, A.A.,Cusack, S. (登録日: 2011-09-28, 公開日: 2011-10-19, 最終更新日: 2023-12-20)

主引用文献

Kowalinski, E.,Lunardi, T.,Mccarthy, A.A.,Louber, J.,Brunel, J.,Grigorov, B.,Gerlier, D.,Cusack, S.
Structural Basis for the Activation of Innate Immune Pattern Recognition Receptor Rig-I by Viral RNA.
Cell(Cambridge,Mass.), 147:423-, 2011

PubMed Abstract: RIG-I is a key innate immune pattern-recognition receptor that triggers interferon expression upon detection of intracellular 5'triphosphate double-stranded RNA (5'ppp-dsRNA) of viral origin. RIG-I comprises N-terminal caspase activation and recruitment domains (CARDs), a DECH helicase, and a C-terminal domain (CTD). We present crystal structures of the ligand-free, autorepressed, and RNA-bound, activated states of RIG-I. Inactive RIG-I has an open conformation with the CARDs sequestered by a helical domain inserted between the two helicase moieties. ATP and dsRNA binding induce a major rearrangement to a closed conformation in which the helicase and CTD bind the blunt end 5'ppp-dsRNA with perfect complementarity but incompatibly with continued CARD binding. We propose that after initial binding of 5'ppp-dsRNA to the flexibly linked CTD, co-operative tight binding of ATP and RNA to the helicase domain liberates the CARDs for downstream signaling. These findings significantly advance our molecular understanding of the activation of innate immune signaling helicases.

PubMed: 22000019
DOI: 10.1016/J.CELL.2011.09.039

実験手法

X-RAY DIFFRACTION (3.4 Å)