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http://purl.uniprot.org/citations/11876640http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11876640http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11876640http://www.w3.org/2000/01/rdf-schema#comment"Arrestin binding to activated, phosphorylated G protein-coupled receptors (GPCRs) represents a critical step in regulation of light- and hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and terminating signaling events. Using a combination of X-ray crystallography, molecular modeling, mutagenesis, and binding analysis, we reveal structural features of arrestin-2 that may enable simultaneous binding to phosphorylated receptor, SH3 domains, phosphoinositides, and beta-adaptin. The structure of full-length arrestin-2 thus provides a uniquely oriented scaffold for assembly of multiple, diverse molecules involved in GPCR signal transduction."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.org/dc/terms/identifier"doi:10.1021/bi015905j"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.org/dc/terms/identifier"doi:10.1021/bi015905j"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Benovic J.L."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Benovic J.L."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Brenner C."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Brenner C."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Kim Y.-M."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Kim Y.-M."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Milano S.K."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Milano S.K."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Pace H.C."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/author"Pace H.C."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/pages"3321-3328"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/pages"3321-3328"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/title"Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/title"Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis."xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/11876640http://purl.uniprot.org/core/volume"41"xsd:string