{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Singh P"],"funding":["NEI NIH HHS","NHLBI NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["14053-62"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2376226"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["283(20)"],"pubmed_abstract":["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 n"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation."],"pmcid":["PMC2376226"],"funding_grant_id":["Y1-GM-1104","EY 08061","P30 EY011373","P30-EY11373","R01 EY008061","HL071818","Y1-CO-1020"],"pubmed_authors":["Palczewski K","Tesmer JJ","Wang B","Maeda T","Singh P"],"additional_accession":[]},"is_claimable":false,"name":"Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation.","description":"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 n","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 May","modification":"2026-05-03T20:12:34.405Z","creation":"2019-03-27T02:45:04Z"},"accession":"S-EPMC2376226","cross_references":{"pubmed":["18339619"],"doi":["10.1074/jbc.m708974200","10.1074/jbc.M708974200"]}}