2ovp

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[[Image:2ovp.gif|left|200px]]
[[Image:2ovp.gif|left|200px]]
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{{Structure
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|PDB= 2ovp |SIZE=350|CAPTION= <scene name='initialview01'>2ovp</scene>, resolution 2.90&Aring;
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The line below this paragraph, containing "STRUCTURE_2ovp", creates the "Structure Box" on the page.
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|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])
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|DOMAIN=
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{{STRUCTURE_2ovp| PDB=2ovp | SCENE= }}
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|RELATEDENTRY=[[2ovq|2OVQ]], [[2ovr|2OVR]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ovp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovp OCA], [http://www.ebi.ac.uk/pdbsum/2ovp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ovp RCSB]</span>
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'''Structure of the Skp1-Fbw7 complex'''
'''Structure of the Skp1-Fbw7 complex'''
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[[Category: Pavletich, N P.]]
[[Category: Pavletich, N P.]]
[[Category: Sowa, M E.]]
[[Category: Sowa, M E.]]
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[[Category: f-box]]
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[[Category: F-box]]
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[[Category: wd40 domain]]
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[[Category: Wd40 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:45:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:55 2008''
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Revision as of 08:45, 4 May 2008

Image:2ovp.gif

Template:STRUCTURE 2ovp

Structure of the Skp1-Fbw7 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

2OVP 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 Sun May 4 11:45:37 2008

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