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

Research output: Contribution to journalArticle

31 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)4888-4897
Number of pages10
JournalEMBO Journal
Volume22
Issue number19
DOIs
Publication statusPublished - Oct 1 2003

All Science Journal Classification (ASJC) codes

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

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