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http://purl.uniprot.org/citations/15537541http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15537541http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15537541http://www.w3.org/2000/01/rdf-schema#comment"The SCF ubiquitin ligase complex regulates diverse cellular functions by ubiquitinating numerous protein substrates. Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex. The crystal structure of the Cand1-Cul1-Roc1 complex shows that Cand1 adopts a highly sinuous superhelical structure, clamping around the elongated SCF scaffold protein Cul1. At one end, a Cand1 beta hairpin protrusion partially occupies the adaptor binding site on Cul1, inhibiting its interactions with the Skp1 adaptor and the substrate-recruiting F box protein subunits. At the other end, two Cand1 HEAT repeats pack against a conserved Cul1 surface cleft and bury a Cul1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cul1 association. Together with biochemical evidence, these structural results elucidate the mechanisms by which Cand1 and Nedd8 regulate the assembly-disassembly cycles of SCF and other cullin-dependent E3 complexes."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2004.10.019"xsd:string
http://purl.uniprot.org/citations/15537541http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2004.10.019"xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Xiong Y."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Xiong Y."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Zheng N."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Zheng N."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Goldenberg S.J."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Goldenberg S.J."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Garbutt K.C."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Garbutt K.C."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Cascio T.C."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Cascio T.C."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Shumway S.D."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/author"Shumway S.D."xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/pages"517-528"xsd:string
http://purl.uniprot.org/citations/15537541http://purl.uniprot.org/core/pages"517-528"xsd:string