2ovr
From Proteopedia
(New page: 200px<br /> <applet load="2ovr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ovr, resolution 2.50Å" /> '''Structure of the Sk...) |
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| - | [[Image:2ovr.gif|left|200px]]<br /> | + | [[Image:2ovr.gif|left|200px]]<br /><applet load="2ovr" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ovr" size=" | + | |
caption="2ovr, resolution 2.50Å" /> | caption="2ovr, resolution 2.50Å" /> | ||
'''Structure of the Skp1-Fbw7-CyclinEdegN complex'''<br /> | '''Structure of the Skp1-Fbw7-CyclinEdegN complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OVR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2OVR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: f-box; wd40 domains; double phosphorylation]] | [[Category: f-box; wd40 domains; double phosphorylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:36:25 2008'' |
Revision as of 13:36, 23 January 2008
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Structure of the Skp1-Fbw7-CyclinEdegN complex
Overview
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.
About this Structure
2OVR is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a Fbw7-Skp1-Cyclin E Complex: Multisite-Phosphorylated Substrate Recognition by SCF Ubiquitin Ligases., Hao B, Oehlmann S, Sowa ME, Harper JW, Pavletich NP, Mol Cell. 2007 Apr 13;26(1):131-43. PMID:17434132
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