1q1o
From Proteopedia
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'''Solution Structure of the PB1 Domain of Cdc24p (Long Form)''' | '''Solution Structure of the PB1 Domain of Cdc24p (Long Form)''' | ||
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[[Category: Yokochi, M.]] | [[Category: Yokochi, M.]] | ||
[[Category: Yoshinaga, S.]] | [[Category: Yoshinaga, S.]] | ||
| - | [[Category: | + | [[Category: Cell polarity]] |
| - | [[Category: | + | [[Category: Opca motif]] |
| - | [[Category: | + | [[Category: Pb1 domain]] |
| - | [[Category: | + | [[Category: Pc motif]] |
| - | [[Category: | + | [[Category: Pccr]] |
| - | [[Category: | + | [[Category: Protein-protein interaction]] |
| - | [[Category: | + | [[Category: Yeast]] |
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Revision as of 02:45, 3 May 2008
Solution Structure of the PB1 Domain of Cdc24p (Long Form)
Overview
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.
About this Structure
1Q1O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The PB1 domain and the PC motif-containing region are structurally similar protein binding modules., Yoshinaga S, Kohjima M, Ogura K, Yokochi M, Takeya R, Ito T, Sumimoto H, Inagaki F, EMBO J. 2003 Oct 1;22(19):4888-97. PMID:14517229 Page seeded by OCA on Sat May 3 05:45:24 2008
