{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Li J"],"pubmed_abstract":["Serine/threonine protein kinase 19 (STK19) has been reported to phosphorylate and activate oncogenic NRAS to promote melanomagenesis. However, concerns have been raised about whether STK19 is a kinase. STK19 has also been identified as a putative factor involved in the transcription-coupled nucleotide excision repair (TC-NER) pathway. In this study, we determined the 1.32 Å crystal structure of human STK19. The structure reveals that STK19 is a winged helix (WH) protein consisting of three tandem WH domains. STK19 binds more strongly to double-stranded DNA and RNA (dsDNA/dsRNA) than to ssDNA. A positively charged patch centered on helix WH3-H1 contributes to dsDNA binding, which is unusual because the WH domain typically uses helix H3 as the recognition helix. Importantly, mutations of the"],"journal":["Scientific reports"],"pagination":["14098"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11189558"],"repository":["biostudies-literature"],"pubmed_title":["Mutations found in cancer patients compromise DNA binding of the winged helix protein STK19."],"pmcid":["PMC11189558"],"pubmed_authors":["Jin G","Li J","Liu K","Hu X","Dong Z","Ma X","Fang S","Wang X"],"additional_accession":[]},"is_claimable":false,"name":"Mutations found in cancer patients compromise DNA binding of the winged helix protein STK19.","description":"Serine/threonine protein kinase 19 (STK19) has been reported to phosphorylate and activate oncogenic NRAS to promote melanomagenesis. However, concerns have been raised about whether STK19 is a kinase. STK19 has also been identified as a putative factor involved in the transcription-coupled nucleotide excision repair (TC-NER) pathway. In this study, we determined the 1.32 Å crystal structure of human STK19. The structure reveals that STK19 is a winged helix (WH) protein consisting of three tandem WH domains. STK19 binds more strongly to double-stranded DNA and RNA (dsDNA/dsRNA) than to ssDNA. A positively charged patch centered on helix WH3-H1 contributes to dsDNA binding, which is unusual because the WH domain typically uses helix H3 as the recognition helix. Importantly, mutations of the","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-05-29T11:42:57.869Z","creation":"2025-04-04T12:47:29.316Z"},"accession":"S-EPMC11189558","cross_references":{"pubmed":["38890355"],"doi":["10.1038/s41598-024-64840-9"]}}