The PB1 domain and the PC motif-containing region are structurally similar protein binding modules

Sosuke Yoshinaga, Motoyuki Kohjima, Kenji Ogura, Masashi Yokochi, Ryu Takeya, Takashi Ito, Hideki Sumimoto, Fuyuhiko Inagaki

研究成果: ジャーナルへの寄稿記事

30 引用 (Scopus)

抄録

The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact ββα-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other.

元の言語英語
ページ(範囲)4888-4897
ページ数10
ジャーナルEMBO Journal
22
発行部数19
DOI
出版物ステータス出版済み - 10 1 2003

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Ubiquitin
Protein Binding
Amino Acid Motifs
Saccharomycetales
Static Electricity
Cell Communication
Proteins
Scaffolds
Dimers
Yeast
Electrostatics
Nuclear magnetic resonance
Polarization

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

これを引用

The PB1 domain and the PC motif-containing region are structurally similar protein binding modules. / Yoshinaga, Sosuke; Kohjima, Motoyuki; Ogura, Kenji; Yokochi, Masashi; Takeya, Ryu; Ito, Takashi; Sumimoto, Hideki; Inagaki, Fuyuhiko.

:: EMBO Journal, 巻 22, 番号 19, 01.10.2003, p. 4888-4897.

研究成果: ジャーナルへの寄稿記事

Yoshinaga, Sosuke ; Kohjima, Motoyuki ; Ogura, Kenji ; Yokochi, Masashi ; Takeya, Ryu ; Ito, Takashi ; Sumimoto, Hideki ; Inagaki, Fuyuhiko. / The PB1 domain and the PC motif-containing region are structurally similar protein binding modules. :: EMBO Journal. 2003 ; 巻 22, 番号 19. pp. 4888-4897.
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abstract = "The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact ββα-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other.",
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AU - Yokochi, Masashi

AU - Takeya, Ryu

AU - Ito, Takashi

AU - Sumimoto, Hideki

AU - Inagaki, Fuyuhiko

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