Your browser doesn't support javascript.
loading
The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3.
Kumanomidou, Taichi; Nishio, Kazuya; Takagi, Kenji; Nakagawa, Tomomi; Suzuki, Atsuo; Yamane, Takashi; Tokunaga, Fuminori; Iwai, Kazuhiro; Murakami, Arisa; Yoshida, Yukiko; Tanaka, Keiji; Mizushima, Tsunehiro.
Afiliação
  • Kumanomidou T; Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya, Japan.
  • Nishio K; Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kouto, Kamigori-cho, Ako-gun, Hyogo, Japan.
  • Takagi K; Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kouto, Kamigori-cho, Ako-gun, Hyogo, Japan.
  • Nakagawa T; Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya, Japan.
  • Suzuki A; Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya, Japan.
  • Yamane T; Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya, Japan.
  • Tokunaga F; Laboratory of Molecular Cell Biology, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan.
  • Iwai K; Graduate School of Medicine, Kyoto University, Yoshida-Konoe-cho, Sakyo-ku, Kyoto, Japan.
  • Murakami A; Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, Japan.
  • Yoshida Y; Ubiquitin Project, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, Japan.
  • Tanaka K; Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, Japan.
  • Mizushima T; Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Kouto, Kamigori-cho, Ako-gun, Hyogo, Japan.
PLoS One ; 10(10): e0140366, 2015.
Article em En | MEDLINE | ID: mdl-26460611
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 ß-sandwich with three helices. Although the overall structure of FBG3 is similar to that of Fbs1, the residues that form the Fbs1 carbohydrate-binding pocket failed to be superposed with the corresponding residues of FBG3. Structure-based mutational analysis shows that distinct hydrogen bond networks of four FBG3 loops, i.e., ß2-ß3, ß5-ß6, ß7-ß8, and ß9-ß10, prevent the formation of the carbohydrate-binding pocket shown in Fbs1.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicoproteínas / Proteínas de Ciclo Celular / Proteínas F-Box / Proteínas do Tecido Nervoso Limite: Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicoproteínas / Proteínas de Ciclo Celular / Proteínas F-Box / Proteínas do Tecido Nervoso Limite: Humans Idioma: En Ano de publicação: 2015 Tipo de documento: Article