4G1T

Crystal structure of interferon-stimulated gene 54

4G1T の概要

• エントリーDOI: 10.2210/pdb4g1t/pdb
• 分子名称: Interferon-induced protein with tetratricopeptide repeats 2 (2 entities in total)
• 機能のキーワード: isg, all alpha helix, antivirus, antiviral protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109460.48

構造登録者

Yang, Z.,Liang, H.,Zhou, Q.,Li, Y.,Chen, H.,Ye, W.,Chen, D.,Fleming, J.,Shu, H.,Liu, Y. (登録日: 2012-07-11, 公開日: 2012-08-15, 最終更新日: 2024-05-29)

主引用文献

Yang, Z.,Liang, H.,Zhou, Q.,Li, Y.,Chen, H.,Ye, W.,Chen, D.,Fleming, J.,Shu, H.,Liu, Y.
Crystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanisms.
Cell Res., 22:1328-1338, 2012

PubMed Abstract: Interferon-stimulated gene 56 (ISG56) family members play important roles in blocking viral replication and regulating cellular functions, however, their underlying molecular mechanisms are largely unclear. Here, we present the crystal structure of ISG54, an ISG56 family protein with a novel RNA-binding structure. The structure shows that ISG54 monomers have 9 tetratricopeptide repeat-like motifs and associate to form domain-swapped dimers. The C-terminal part folds into a super-helical structure and has an extensively positively-charged nucleotide-binding channel on its inner surface. EMSA results show that ISG54 binds specifically to some RNAs, such as adenylate uridylate (AU)-rich RNAs, with or without 5' triphosphorylation. Mutagenesis and functional studies show that this RNA-binding ability is important to its antiviral activity. Our results suggest a new mechanism underlying the antiviral activity of this interferon-inducible gene 56 family member.

PubMed: 22825553
DOI: 10.1038/cr.2012.111

実験手法

X-RAY DIFFRACTION (2.8 Å)