RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18178622http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18178622http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18178622http://www.w3.org/2000/01/rdf-schema#comment"Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major conformational states: apo, intermediate, and closed. The allosteric network is disrupted by a single site mutation (Y204A), which also decouples the cooperativity of ligand binding. Because protein kinase A is the prototype for the entire kinome, these findings may serve as a paradigm for describing long-range coupling in other protein kinases."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0709214104"xsd:string
http://purl.uniprot.org/citations/18178622http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0709214104"xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Taylor S.S."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Taylor S.S."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Masterson L.R."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Masterson L.R."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Veglia G."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Veglia G."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Mascioni A."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Mascioni A."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Traaseth N.J."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/author"Traaseth N.J."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/pages"506-511"xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/pages"506-511"xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/title"Allosteric cooperativity in protein kinase A."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/title"Allosteric cooperativity in protein kinase A."xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/18178622http://purl.uniprot.org/core/volume"105"xsd:string