1q1o
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(New page: 200px<br /><applet load="1q1o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q1o" /> '''Solution Structure of the PB1 Domain of Cdc2...)
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Revision as of 22:11, 20 November 2007
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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
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