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http://purl.uniprot.org/citations/18339619http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18339619http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18339619http://www.w3.org/2000/01/rdf-schema#comment"G protein-coupled receptor (GPCR) kinases (GRKs) phosphorylate activated heptahelical receptors, leading to their uncoupling from G proteins. Here we report six crystal structures of rhodopsin kinase (GRK1), revealing not only three distinct nucleotide-binding states of a GRK but also two key structural elements believed to be involved in the recognition of activated GPCRs. The first is the C-terminal extension of the kinase domain, which was observed in all nucleotide-bound GRK1 structures. The second is residues 5-30 of the N terminus, observed in one of the GRK1.(Mg2+)2.ATP structures. The N terminus was also clearly phosphorylated, leading to the identification of two novel phosphorylation sites by mass spectral analysis. Co-localization of the N terminus and the C-terminal extension near the hinge of the kinase domain suggests that activated GPCRs stimulate kinase activity by binding to this region to facilitate full closure of the kinase domain."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m708974200"xsd:string
http://purl.uniprot.org/citations/18339619http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m708974200"xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Wang B."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Wang B."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Maeda T."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Maeda T."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Singh P."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Singh P."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Palczewski K."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Palczewski K."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Tesmer J.J."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/author"Tesmer J.J."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/pages"14053-14062"xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/pages"14053-14062"xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/title"Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/title"Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation."xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18339619http://purl.uniprot.org/core/volume"283"xsd:string