6L1W

Zinc-finger Antiviral Protein (ZAP) bound to RNA

6L1W の概要

• エントリーDOI: 10.2210/pdb6l1w/pdb
• 分子名称: Zinc finger CCCH-type antiviral protein 1, RNA (5'-R(*CP*GP*UP*CP*GP*U)-3'), ZINC ION, ... (4 entities in total)
• 機能のキーワード: rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28524.07

構造登録者

Luo, X.,Wang, X.,Gao, Y.,Zhu, J.,Liu, S.,Gao, G.,Gao, P. (登録日: 2019-09-30, 公開日: 2020-01-01, 最終更新日: 2023-11-22)

主引用文献

Luo, X.,Wang, X.,Gao, Y.,Zhu, J.,Liu, S.,Gao, G.,Gao, P.
Molecular Mechanism of RNA Recognition by Zinc-Finger Antiviral Protein.
Cell Rep, 30:46-52.e4, 2020

PubMed Abstract: Zinc-finger antiviral protein (ZAP) is a host antiviral factor that specifically restricts a wide range of viruses. ZAP selectively binds to CG-dinucleotide-enriched RNA sequences and recruits multiple RNA degradation machines to degrade target viral RNA. However, the molecular mechanism and structural basis for ZAP recognition of specific RNA are not clear. Here, we report the crystal structure of the ZAP N-terminal domain bound to a CG-rich single-stranded RNA, providing the molecular basis for its specific recognition of a CG dinucleotide and additional guanine and cytosine. The four zinc fingers of ZAP adopt a unique architecture and form extensive interactions with RNA. Mutations of both protein and RNA at the RNA-ZAP interacting surface reduce the in vitro binding affinity and cellular antiviral activity. This work reveals the molecular mechanism of ZAP recognition of specific target RNA and also provides insights into the mechanism by which ZAP coordinates downstream RNA degradation processes.

PubMed: 31914396
DOI: 10.1016/j.celrep.2019.11.116

実験手法

X-RAY DIFFRACTION (2.194 Å)