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| {{STRUCTURE_2ovq| PDB=2ovq | SCENE= }} | | {{STRUCTURE_2ovq| PDB=2ovq | SCENE= }} |
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| '''Structure of the Skp1-Fbw7-CyclinEdegC complex'''
| | ===Structure of the Skp1-Fbw7-CyclinEdegC complex=== |
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| ==Overview==
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| The ubiquitin-mediated proteolysis of cyclin E plays a central role in cell-cycle progression, and cyclin E accumulation is a common event in cancer. Cyclin E degradation is triggered by multisite phosphorylation, which induces binding to the SCF(Fbw7) ubiquitin ligase complex. Structures of the Skp1-Fbw7 complex bound to cyclin E peptides identify a doubly phosphorylated pThr380/pSer384 cyclin E motif as an optimal, high-affinity degron and a singly phosphorylated pThr62 motif as a low-affinity one. Biochemical data indicate that the closely related yeast SCF(Cdc4) complex recognizes the multisite phosphorylated Sic1 substrate similarly and identify three doubly phosphorylated Sic1 degrons, each capable of high-affinity interactions with two Cdc4 phosphate binding sites. A model that explains the role of multiple cyclin E/Sic1 degrons is provided by the findings that Fbw7 and Cdc4 dimerize, that Fbw7 dimerization enhances the turnover of a weakly associated cyclin E in vivo, and that Cdc4 dimerization increases the rate and processivity of Sic1 ubiquitination in vitro. | | The line below this paragraph, {{ABSTRACT_PUBMED_17434132}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17434132 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17434132}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: F-box]] | | [[Category: F-box]] |
| [[Category: Wd40 domain]] | | [[Category: Wd40 domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:45:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:35:00 2008'' |
