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http://purl.uniprot.org/citations/22483108http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22483108http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22483108http://www.w3.org/2000/01/rdf-schema#comment"The viral oncoprotein E6 is an essential factor for cervical cancers induced by "high-risk" mucosal HPV. Among other oncogenic activities, E6 recruits the ubiquitin ligase E6AP to promote the ubiquitination and subsequent proteasomal degradation of p53. E6 is prone to self-association, which long precluded its structural analysis. Here we found that E6 specifically dimerizes through its N-terminal domain and that disruption of the dimer interface strongly increases E6 solubility. This allowed us to raise structural data covering the entire HPV16 E6 protein, including the high-resolution NMR structures of the two zinc-binding domains of E6 and a robust data-driven model structure of the N-terminal domain homodimer. Interestingly, homodimer interface mutations that disrupt E6 self-association also inactivate E6-mediated p53 degradation. These data suggest that E6 needs to self-associate via its N-terminal domain to promote the polyubiquitination of p53 by E6AP."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2012.02.001"xsd:string
http://purl.uniprot.org/citations/22483108http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2012.02.001"xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Atkinson A."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Atkinson A."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Rybin V."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Rybin V."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Kieffer B."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Kieffer B."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Boulade-Ladame C."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Boulade-Ladame C."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Chappelle A."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Chappelle A."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Trave G."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Trave G."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Zanier K."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"Zanier K."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"ould M'hamed ould Sidi A."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/author"ould M'hamed ould Sidi A."xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/22483108http://purl.uniprot.org/core/name"Structure"xsd:string