RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/23001005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23001005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23001005http://www.w3.org/2000/01/rdf-schema#comment"The human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3, referred to as A3) proteins are cellular cytidine deaminases that potently restrict retrovirus replication. However, HIV-1 viral infectivity factor (Vif) counteracts the antiviral activity of most A3 proteins by targeting them for proteasomal degradation. To date, the structure of an A3 protein containing a Vif-binding interface has not been solved. Here, we report a high-resolution crystal structure of APOBEC3C and identify the HIV-1 Vif-interaction interface. Extensive structure-guided mutagenesis revealed the role of a shallow cavity composed of hydrophobic or negatively charged residues between the α2 and α3 helices. This region is distant from the DPD motif (residues 128-130) of APOBEC3G that participates in HIV-1 Vif interaction. These findings provide insight into Vif-A3 interactions and could lead to the development of new pharmacologic anti-HIV-1 compounds."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2378"xsd:string
http://purl.uniprot.org/citations/23001005http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2378"xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Nakashima M."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Nakashima M."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Suzuki A."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Suzuki A."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Yamane T."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Yamane T."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Watanabe N."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Watanabe N."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Kitamura S."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Kitamura S."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Imahashi M."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Imahashi M."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Iwatani Y."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Iwatani Y."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Kurosawa T."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Kurosawa T."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Naganawa Y."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Naganawa Y."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Ode H."xsd:string
http://purl.uniprot.org/citations/23001005http://purl.uniprot.org/core/author"Ode H."xsd:string