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http://purl.uniprot.org/citations/32913000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32913000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32913000http://www.w3.org/2000/01/rdf-schema#comment"Cyclic guanosine monophosphate (GMP)-adenosine monophosphate (AMP) synthase (cGAS) recognizes cytosolic foreign or damaged DNA to activate the innate immune response to infection, inflammatory diseases, and cancer. By contrast, cGAS reactivity against self-DNA in the nucleus is suppressed by chromatin tethering. We report a 3.3-angstrom-resolution cryo-electron microscopy structure of cGAS in complex with the nucleosome core particle. The structure reveals that cGAS uses two conserved arginines to anchor to the nucleosome acidic patch. The nucleosome-binding interface exclusively occupies the strong double-stranded DNA (dsDNA)-binding surface on cGAS and sterically prevents cGAS from oligomerizing into the functionally active 2:2 cGAS-dsDNA state. These findings provide a structural basis for how cGAS maintains an inhibited state in the nucleus and further exemplify the role of the nucleosome in regulating diverse nuclear protein functions."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.org/dc/terms/identifier"doi:10.1126/science.abd0609"xsd:string
http://purl.uniprot.org/citations/32913000http://purl.org/dc/terms/identifier"doi:10.1126/science.abd0609"xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Liu P."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Liu P."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Zhang Q."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Zhang Q."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"McGinty R.K."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"McGinty R.K."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Boyer J.A."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Boyer J.A."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Cesmat A.P."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Cesmat A.P."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Spangler C.J."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Spangler C.J."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Strauss J.D."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/author"Strauss J.D."xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/pages"450-454"xsd:string
http://purl.uniprot.org/citations/32913000http://purl.uniprot.org/core/pages"450-454"xsd:string