{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Youle RL"],"funding":["Medical Research Council","The Francis Crick Institute","National Institute for Health Research (NIHR)","Wellcome Trust","Wellcome Trust Senior Research"],"pagination":["gkaf1360"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12709174"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(22)"],"pubmed_abstract":["Zinc finger antiviral protein (ZAP) is a cytoplasmic protein central to host innate immunity to viral infection. ZAP has no intrinsic catalytic activity but inhibits viral replication by binding to CpG dinucleotides in cytoplasmic viral RNA and recruiting other factors to inhibit protein synthesis and target the RNA for degradation. KHNYN is a ZAP-binding protein required for ZAP-restriction of CpG-rich viral genomes. It contains an extended diKH, PIN nuclease, and CUElike domain, each of which are required for ZAP restriction of viral replication. Here, we report a structural, enzymological, and virological study of KHNYN's essential PIN nuclease domain. Our crystal structure reveals an extended PIN domain (ex-PIN) containing a conserved N-terminal arm region required for domain stability"],"journal":["Nucleic acids research"],"pubmed_title":["KHNYN is a manganese-dependent endoribonuclease required for ZAP-mediated antiviral restriction."],"pmcid":["PMC12709174"],"funding_grant_id":["WT098049AIA","MR/S000844/1","CC2029","MR/W018519/1"],"pubmed_authors":["Youle RL","Thompson B","Bouton C","Taylor IA","Morris ER","Swanson CM","Neil SJD","Brudenell EL","Lista MJ"],"additional_accession":[]},"is_claimable":false,"name":"KHNYN is a manganese-dependent endoribonuclease required for ZAP-mediated antiviral restriction.","description":"Zinc finger antiviral protein (ZAP) is a cytoplasmic protein central to host innate immunity to viral infection. ZAP has no intrinsic catalytic activity but inhibits viral replication by binding to CpG dinucleotides in cytoplasmic viral RNA and recruiting other factors to inhibit protein synthesis and target the RNA for degradation. KHNYN is a ZAP-binding protein required for ZAP-restriction of CpG-rich viral genomes. It contains an extended diKH, PIN nuclease, and CUElike domain, each of which are required for ZAP restriction of viral replication. Here, we report a structural, enzymological, and virological study of KHNYN's essential PIN nuclease domain. Our crystal structure reveals an extended PIN domain (ex-PIN) containing a conserved N-terminal arm region required for domain stability","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-06T03:58:02.029Z","creation":"2026-05-25T03:12:11.956Z"},"accession":"S-EPMC12709174","cross_references":{"pubmed":["41404804"],"doi":["10.1093/nar/gkaf1360"]}}