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2QFB

Crystal structure of the regulatory domain of human RIG-I with bound Zn

2QFB の概要
エントリーDOI10.2210/pdb2qfb/pdb
関連するPDBエントリー2QFD
分子名称Probable ATP-dependent RNA helicase DDX58, ZINC ION (3 entities in total)
機能のキーワードzinc finger, alternative splicing, antiviral defense, atp-binding, helicase, hydrolase, immune response, innate immunity, interferon induction, nucleotide-binding, polymorphism, rna-binding, ubl conjugation
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm: O95786
タンパク質・核酸の鎖数10
化学式量合計169189.07
構造登録者
Cui, S.,Lammens, A.,Lammens, K.,Hopfner, K.P. (登録日: 2007-06-27, 公開日: 2008-02-12, 最終更新日: 2024-11-20)
主引用文献Cui, S.,Eisenacher, K.,Kirchhofer, A.,Brzozka, K.,Lammens, A.,Lammens, K.,Fujita, T.,Conzelmann, K.K.,Krug, A.,Hopfner, K.P.
The C-Terminal Regulatory Domain Is the RNA 5'-Triphosphate Sensor of RIG-I.
Mol.Cell, 29:169-179, 2008
Cited by
PubMed Abstract: The ATPase RIG-I senses viral RNAs that contain 5'-triphosphates in the cytoplasm. It initiates a signaling cascade that activates innate immune response by interferon and cytokine production, providing essential antiviral protection for the host. The mode of RNA 5'-triphosphate sensing by RIG-I remains elusive. We show that the C-terminal regulatory domain RD of RIG-I binds viral RNA in a 5'-triphosphate-dependent manner and activates the RIG-I ATPase by RNA-dependent dimerization. The crystal structure of RD reveals a zinc-binding domain that is structurally related to GDP/GTP exchange factors of Rab-like GTPases. The zinc coordination site is essential for RIG-I signaling and is also conserved in MDA5 and LGP2, suggesting related RD domains in all three enzymes. Structure-guided mutagenesis identifies a positively charged groove as likely 5'-triphosphate-binding site of RIG-I. This groove is distinct in MDA5 and LGP2, raising the possibility that RD confers ligand specificity.
PubMed: 18243112
DOI: 10.1016/j.molcel.2007.10.032
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 2qfb
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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