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http://purl.uniprot.org/citations/31792451http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31792451http://www.w3.org/2000/01/rdf-schema#comment"HIV-1 virion infectivity factor (Vif) promotes degradation of the antiviral APOBEC3 (A3) proteins through the host ubiquitin-proteasome pathway to enable viral immune evasion. Disrupting Vif-A3 interactions to reinstate the A3-catalyzed suppression of human immunodeficiency virus type 1 (HIV-1) replication is a potential approach for antiviral therapeutics. However, the molecular mechanisms by which Vif recognizes A3 proteins remain elusive. Here we report a cryo-EM structure of the Vif-targeted C-terminal domain of human A3F in complex with HIV-1 Vif and the cellular cofactor core-binding factor beta (CBFβ) at 3.9-Å resolution. The structure shows that Vif and CBFβ form a platform to recruit A3F, revealing a direct A3F-recruiting role of CBFβ beyond Vif stabilization, and captures multiple independent A3F-Vif interfaces. Together with our biochemical and cellular studies, our structural findings establish the molecular determinants that are critical for Vif-mediated neutralization of A3F and provide a comprehensive framework of how HIV-1 Vif hijacks the host protein degradation machinery to counteract viral restriction by A3F."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.org/dc/terms/identifier"doi:10.1038/s41594-019-0343-6"xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Nguyen H.C."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Pathak V.K."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Xiong Y."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Zhang K."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Cheng T.C."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Desimmie B.A."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/author"Ziegler S.J."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/pages"1176-1183"xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/title"Structural basis of antagonism of human APOBEC3F by HIV-1 Vif."xsd:string
http://purl.uniprot.org/citations/31792451http://purl.uniprot.org/core/volume"26"xsd:string
http://purl.uniprot.org/citations/31792451http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31792451
http://purl.uniprot.org/citations/31792451http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31792451
http://purl.uniprot.org/uniprot/#_F2YHL7-mappedCitation-31792451http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31792451
http://purl.uniprot.org/uniprot/#_A0A288CG30-mappedCitation-31792451http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31792451
http://purl.uniprot.org/uniprot/#_B4DGW8-mappedCitation-31792451http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31792451
http://purl.uniprot.org/uniprot/#_A8K719-mappedCitation-31792451http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31792451