ArticleThe EMBO journal2003
The PB1 domain and the PC motif-containing region are structurally similar protein binding modules.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Phylogenetic and Structural Analysis of NIN-Like Proteins With a Type I/II PB1 Domain That Regulates Oligomerization for Nitrate Response.Frontiers in plant science · 2021Article
- A Split-Ubiquitin Based Strategy Selecting for Protein Complex-Interfering Mutations.G3 (Bethesda, Md.) · 2016Article
- Essential role of the NH2-terminal region of Cdc24 guanine nucleotide exchange factor in its initial polarized localization in Saccharomyces cerevisiae.Eukaryotic cell · 2012Article
- Solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42.The Journal of biological chemistry · 2010Article
- The structural and functional determinants of the Axin and Dishevelled DIX domains.BMC structural biology · 2009Article
- Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding.The EMBO journal · 2007Article
- Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle.Molecular and cellular biology · 2005Article
- Activation and assembly of the NADPH oxidase: a structural perspective.The Biochemical journal · 2005Review
- Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth.Molecular biology of the cell · 2005Article
- Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation.Molecular and cellular biology · 2004Article
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8 authors.
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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 betabetaalpha-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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