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http://purl.uniprot.org/citations/7798208http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7798208http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7798208http://www.w3.org/2000/01/rdf-schema#comment"The human immunodeficiency virus, type 1 (HIV-1) genome encodes a 15-kDa accessory gene product, Vpr, that is essential for virus replication in primary monocytes/macrophages. Being present in the virion, Vpr is believed to function in the early phases of HIV-1 replication, including nuclear migration of the pre-integration complex and/or transcription of the provirus genome. By gel filtration analysis of highly purified Vpr protein and its mutants, we demonstrate that HIV-1 Vpr exists as an oligomer. The N-terminal domain of Vpr (amino acids (aa) 1-42) is sufficient for oligomerization; however, deletion of aa 36-76 from Vpr disrupts oligomerization, suggesting that aa 36-42 are critical for Vpr oligomerization. As a result of Vpr oligomerization, basic aa residues within Vpr aa 1-73 are highly resistant to trypsin digestion, while those within Vpr aa 74-96 are easily accessible. Mutations within the leucine-/isoleucine-rich domain (aa 60-81), which was previously identified to be involved in Vpr interaction with a host cellular protein, rendered Arg62 more susceptible to trypsin digestion. Thus, the Vpr oligomeric structure must be extended into this domain. These results suggest a novel feature of HIV-1 Vpr that may be important for its functions."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)31610-7"xsd:string
http://purl.uniprot.org/citations/7798208http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)31610-7"xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Wang L."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Wang L."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Mukherjee S."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Mukherjee S."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Zhao L.J."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Zhao L.J."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Narayan O."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/author"Narayan O."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/pages"32131-32137"xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/pages"32131-32137"xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/title"Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/title"Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain."xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7798208http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7798208http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7798208
http://purl.uniprot.org/citations/7798208http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7798208