4H22

Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1

4H22 の概要

• エントリーDOI: 10.2210/pdb4h22/pdb
• 関連するPDBエントリー: 2q6q
• 分子名称: Leucine-rich repeat flightless-interacting protein 1 (2 entities in total)
• 機能のキーワード: nucleic acid sensor, flightless-1, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q32MZ4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49599.78

構造登録者

Nguyen, J.B.,Modis, Y. (登録日: 2012-09-11, 公開日: 2012-11-07, 最終更新日: 2023-09-20)

主引用文献

Nguyen, J.B.,Modis, Y.
Crystal structure of the dimeric coiled-coil domain of the cytosolic nucleic acid sensor LRRFIP1.
J.Struct.Biol., 181:82-88, 2013

PubMed Abstract: LRRFIP1 binds cytoplasmic double-stranded DNA and RNA and interacts with FLI, the mammalian homolog of Drosophila flightless I, through a highly conserved 87-amino acid domain. Upon binding nucleic acid ligands, LRRFIP1 recruits and activates β-catenin, leading to the IRF3-dependent production of type I interferon. However, the molecular mechanism of LRRFIP1 signaling is not well understood. Here we show that the FLI-interacting domain of LRRFIP1 forms a classic parallel, homodimeric coiled coil with 10 heptad repeats and 22 helical turns. The coiled coil domain is also a dimer in solution. However, a longer LRRFIP1 construct spanning the coiled coil and DNA binding domains assembles into higher order oligomers in solution. The structure of LRRFIP1-CC constitutes a valuable tool for probing the mechanism of LRRFIP1 signaling and for structural studies of larger LRRFIP1 constructs.

PubMed: 23099021
DOI: 10.1016/j.jsb.2012.10.006

実験手法

X-RAY DIFFRACTION (2.89 Å)