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http://purl.uniprot.org/citations/35061538http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35061538http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35061538http://www.w3.org/2000/01/rdf-schema#comment"Human cytomegalovirus (HCMV) encodes G protein-coupled receptors (GPCRs) US28 and US27, which facilitate viral pathogenesis through engagement of host G proteins. Here we report cryo-electron microscopy structures of US28 and US27 forming nonproductive and productive complexes with Gi and Gq, respectively, exhibiting unusual features with functional implications. The "orphan" GPCR US27 lacks a ligand-binding pocket and has captured a guanosine diphosphate-bound inactive Gi through a tenuous interaction. The docking modes of CX3CL1-US28 and US27 to Gi favor localization to endosome-like curved membranes, where US28 and US27 can function as nonproductive Gi sinks to attenuate host chemokine-dependent Gi signaling. The CX3CL1-US28-Gq/11 complex likely represents a trapped intermediate during productive signaling, providing a view of a transition state in GPCR-G protein coupling for signaling. Our collective results shed new insight into unique G protein-mediated HCMV GPCR structural mechanisms, compared to mammalian GPCR counterparts, for subversion of host immunity."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.abl5442"xsd:string
http://purl.uniprot.org/citations/35061538http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.abl5442"xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Garcia K.C."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Garcia K.C."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Kobilka B.K."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Kobilka B.K."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Maeda S."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Maeda S."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Qu Q."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Qu Q."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Skiniotis G."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Skiniotis G."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Tsutsumi N."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Tsutsumi N."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Waghray D."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Waghray D."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Kato H.E."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Kato H.E."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Dror R.O."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Dror R.O."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Panova O."xsd:string
http://purl.uniprot.org/citations/35061538http://purl.uniprot.org/core/author"Panova O."xsd:string