1QWT

Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain

1QWT の概要

• エントリーDOI: 10.2210/pdb1qwt/pdb
• 分子名称: Interferon regulatory factor 3, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q14653
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57079.37

構造登録者

Qin, B.Y. (登録日: 2003-09-03, 公開日: 2003-10-14, 最終更新日: 2024-10-30)

主引用文献

Qin, B.Y.,Liu, C.,Lam, S.S.,Srinath, H.,Delston, R.,Correia, J.J.,Derynck, R.,Lin, K.
Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus induced phospho-activation
Nat.Struct.Biol., 10:913-921, 2003

PubMed Abstract: IRF-3, a member of the interferon regulatory factor (IRF) family of transcription factors, functions as a molecular switch for antiviral activity. IRF-3 uses an autoinhibitory mechanism to suppress its transactivation potential in uninfected cells, and virus infection induces phosphorylation and activation of IRF-3 to initiate the antiviral responses. The crystal structure of the IRF-3 transactivation domain reveals a unique autoinhibitory mechanism, whereby the IRF association domain and the flanking autoinhibitory elements condense to form a hydrophobic core. The structure suggests that phosphorylation reorganizes the autoinhibitory elements, leading to unmasking of a hydrophobic active site and realignment of the DNA binding domain for transcriptional activation. IRF-3 exhibits marked structural and surface electrostatic potential similarity to the MH2 domain of the Smad protein family and the FHA domain, suggesting a common molecular mechanism of action among this superfamily of signaling mediators.

PubMed: 14555996
DOI: 10.1038/nsb1002

実験手法

X-RAY DIFFRACTION (2.1 Å)