1q1o: Difference between revisions
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'''Solution Structure of the PB1 Domain of Cdc24p (Long Form)''' | {{Structure | ||
|PDB= 1q1o |SIZE=350|CAPTION= <scene name='initialview01'>1q1o</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= Cdc24p ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Solution Structure of the PB1 Domain of Cdc24p (Long Form)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Q1O is a [ | 1Q1O is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14517229 14517229] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: yeast]] | [[Category: yeast]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:31:53 2008'' | ||
Revision as of 14:32, 20 March 2008
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| Gene: | Cdc24p (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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