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http://purl.uniprot.org/citations/11157746http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11157746http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11157746http://www.w3.org/2000/01/rdf-schema#comment"Human cytomegalovirus (HCMV) encodes several genes that disrupt the major histocompatibility complex (MHC) class I antigen presentation pathway. We recently described the HCMV-encoded US6 gene product, a 23 kDa endoplasmic reticulum (ER)-resident type I integral membrane protein that binds to the transporter associated with antigen processing (TAP), inhibits peptide translocation and prevents MHC class I assembly. The functional consequence of this inhibition is to prevent the cell surface expression of class I bound viral peptides and their recognition by HCMV-specific cytotoxic T cells. Here we describe a novel mechanism of action for US6. We demonstrate that US6 inhibits the binding of ATP by TAP1. This is a conformational effect, as the ER lumenal domain of US6 is sufficient to inhibit ATP binding by the cytosolic nucleotide binding domain of TAP1. US6 also stabilizes TAP at 37 degrees C and prevents conformational rearrangements induced by peptide binding. Our findings suggest that the association of US6 with TAP stabilizes a conformation in TAP1 that prevents ATP binding and subsequent peptide translocation."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.3.387"xsd:string
http://purl.uniprot.org/citations/11157746http://purl.org/dc/terms/identifier"doi:10.1093/emboj/20.3.387"xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/author"Lehner P.J."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/author"Lehner P.J."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/author"Hewitt E.W."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/author"Hewitt E.W."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/author"Gupta S.S."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/author"Gupta S.S."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/pages"387-396"xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/pages"387-396"xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/title"The human cytomegalovirus gene product US6 inhibits ATP binding by TAP."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/title"The human cytomegalovirus gene product US6 inhibits ATP binding by TAP."xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/11157746http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/11157746http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11157746
http://purl.uniprot.org/citations/11157746http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11157746
http://purl.uniprot.org/citations/11157746http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11157746
http://purl.uniprot.org/citations/11157746http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11157746