Structure and ligand recognition of the PB1 domain: A novel protein module binding to the PC motif

Hiroaki Terasawa, Yukiko Noda, Takashi Ito, Hideki Hatanaka, Saori Ichikawa, Kenji Ogura, Hideki Sumimoto, Fuyuhiko Inagaki

Research output: Contribution to journalArticlepeer-review

58 Citations (Scopus)

Abstract

PB1 domains are novel protein modules capable of binding to target proteins that contain PC motifs. We report here the NMR structure and ligand-binding site of the PB1 domain of the cell polarity establishment protein, Bem1p. In addition, we identify the topology of the PC motif-containing region of Cdc24p by NMR, another cell polarity establishment protein that interacts with Bem1p. The PC motif-containing region is a structural domain offering a scaffold to the PC motif. The chemical shift perturbation experiment and the mutagenesis study show that the PC motif is a major structural element that binds to the PB1 domain. A structural database search reveals close similarity between the Bem1p PB1 domain and the c-Raf1 Ras-binding domain. However, these domains are functionally distinct from each other.

Original languageEnglish
Pages (from-to)3947-3956
Number of pages10
JournalEMBO Journal
Volume20
Issue number15
DOIs
Publication statusPublished - Aug 1 2001

All Science Journal Classification (ASJC) codes

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

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