2ovq
From Proteopedia
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| - | [[Image:2ovq.gif|left|200px]] | + | [[Image:2ovq.gif|left|200px]] |
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| - | '''Structure of the Skp1-Fbw7-CyclinEdegC complex''' | + | {{Structure |
| + | |PDB= 2ovq |SIZE=350|CAPTION= <scene name='initialview01'>2ovq</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= SKP1A, EMC19, OCP2, SKP1, TCEB1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), FBXW7, FBW7, FBX30, SEL10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of the Skp1-Fbw7-CyclinEdegC complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OVQ is a [ | + | 2OVQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17434132 17434132] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: f-box; wd40 domains; double phosphorylation]] | [[Category: f-box; wd40 domains; double phosphorylation]] | ||
| - | ''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 18:05:11 2008'' |
Revision as of 16:05, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SKP1A, EMC19, OCP2, SKP1, TCEB1L (Homo sapiens), FBXW7, FBW7, FBX30, SEL10 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the Skp1-Fbw7-CyclinEdegC 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
2OVQ is a Protein complex structure of sequences from Homo sapiens. 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
Page seeded by OCA on Thu Mar 20 18:05:11 2008
