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Summary

Description
English: Left: Molecular mechanism of zinc-finger antiviral protein (ZAP) recognition of specific target RNA and also the mechanism by which ZAP coordinates downstream RNA degradation processes. 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. Right: 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.
Date
Source

Xiu Luo, Xinlu Wang, Yina Gao, Jingpeng Zhu, Songqing Liu, Guangxia Gao, Pu Gao, Molecular Mechanism of RNA Recognition by Zinc-Finger Antiviral Protein, Cell Reports, Volume 30, Issue 1, 2020, Pages 46-52.e4, ISSN 2211-1247, https://doi.org/10.1016/j.celrep.2019.11.116 .

( https://www.sciencedirect.com/science/article/pii/S2211124719316390 )
Author Xiu Luo, Xinlu Wang, Yina Gao, Jingpeng Zhu, Songqing Liu, Guangxia Gao, and Pu Gao

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Molecular mechanism of zinc-finger antiviral protein (ZAP) recognition of specific target RNA and also the mechanism by which ZAP coordinates downstream RNA degradation processes.

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20 January 2020

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