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Significance Zinc finger antiviral protein (ZAP) protects cells from infection by diverse RNA viruses through its ability to specifically detect and deplete viral RNAs that have a greater frequency of CG dinucleotides than host messenger RNAs. We solved an X-ray crystal structure of the domain of ZAP that recognizes RNA and found that a crucial component of RNA recognition by ZAP is a pocket on the protein surface that can accommodate a CG dinucleotide but no other dinucleotides. The structure explains in atomic detail how ZAP is able to selectively recognize CG-rich viral RNAs as foreign and thereby provide hosts with a defense against viral infection.

Structure of the zinc-finger antiviral protein in complex with RNA reveals a mechanism for selective targeting of CG-rich viral sequences