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http://purl.uniprot.org/citations/17962520http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17962520http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17962520http://www.w3.org/2000/01/rdf-schema#comment"Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors constitute the largest family of eukaryotic signal transduction proteins that communicate across the membrane. We report the crystal structure of a human beta2-adrenergic receptor-T4 lysozyme fusion protein bound to the partial inverse agonist carazolol at 2.4 angstrom resolution. The structure provides a high-resolution view of a human G protein-coupled receptor bound to a diffusible ligand. Ligand-binding site accessibility is enabled by the second extracellular loop, which is held out of the binding cavity by a pair of closely spaced disulfide bridges and a short helical segment within the loop. Cholesterol, a necessary component for crystallization, mediates an intriguing parallel association of receptor molecules in the crystal lattice. Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopsin as a template model for this large receptor family."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.org/dc/terms/identifier"doi:10.1126/science.1150577"xsd:string
http://purl.uniprot.org/citations/17962520http://purl.org/dc/terms/identifier"doi:10.1126/science.1150577"xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Kuhn P."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Kuhn P."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Kobilka B.K."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Kobilka B.K."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Stevens R.C."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Stevens R.C."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Cherezov V."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Cherezov V."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Kobilka T.S."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Kobilka T.S."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Choi H.-J."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Choi H.-J."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Hanson M.A."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Hanson M.A."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Rosenbaum D.M."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Rosenbaum D.M."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Rasmussen S.G.F."xsd:string
http://purl.uniprot.org/citations/17962520http://purl.uniprot.org/core/author"Rasmussen S.G.F."xsd:string