{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(10)"],"submitter":["Kumanomidou T"],"pubmed_abstract":["The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in diverse cellular processes and is one of the best-characterized ubiquitin ligases. F-box proteins determine the substrate specificities of SCF ubiquitin ligases. Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3. Here we determined the crystal structure of the Skp1-FBG3 complex at a resolution of 2.6 Å. The substrate-binding domain of FBG3 is composed of a 10-stranded antiparallel β-sandwich with three helices. Although the overall structure of FBG3 is similar to that of Fbs1,"],"journal":["PloS one"],"pagination":["e0140366"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4603797"],"repository":["biostudies-literature"],"pubmed_title":["The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3."],"pmcid":["PMC4603797"],"pubmed_authors":["Suzuki A","Tokunaga F","Nishio K","Kumanomidou T","Yamane T","Murakami A","Nakagawa T","Mizushima T","Takagi K","Yoshida Y","Tanaka K","Iwai K"],"additional_accession":[]},"is_claimable":false,"name":"The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3.","description":"The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in diverse cellular processes and is one of the best-characterized ubiquitin ligases. F-box proteins determine the substrate specificities of SCF ubiquitin ligases. Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3. Here we determined the crystal structure of the Skp1-FBG3 complex at a resolution of 2.6 Å. The substrate-binding domain of FBG3 is composed of a 10-stranded antiparallel β-sandwich with three helices. Although the overall structure of FBG3 is similar to that of Fbs1,","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015","modification":"2026-04-07T19:39:46.462Z","creation":"2019-03-26T23:27:43Z"},"accession":"S-EPMC4603797","cross_references":{"pubmed":["26460611"],"doi":["10.1371/journal.pone.0140366"]}}