1q1o: Difference between revisions
New page: left|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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[[Image:1q1o.jpg|left|200px]]<br /><applet load="1q1o" size=" | [[Image:1q1o.jpg|left|200px]]<br /><applet load="1q1o" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Solution Structure of the PB1 Domain of Cdc24p (Long Form)'''<br /> | '''Solution Structure of the PB1 Domain of Cdc24p (Long Form)'''<br /> | ||
==Overview== | ==Overview== | ||
The PC motif is evolutionarily conserved together with the PB1 domain, a | 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== | ==About this Structure== | ||
1Q1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | 1Q1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1O OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: yeast]] | [[Category: yeast]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:56 2008'' | ||
Revision as of 15:34, 21 February 2008
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Solution Structure of the PB1 Domain of Cdc24p (Long Form)
OverviewOverview
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 StructureAbout this Structure
1Q1O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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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