2ovr
From Proteopedia
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|PDB= 2ovr |SIZE=350|CAPTION= <scene name='initialview01'>2ovr</scene>, resolution 2.50Å | |PDB= 2ovr |SIZE=350|CAPTION= <scene name='initialview01'>2ovr</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene> |
|ACTIVITY= | |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]) | |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]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[2ovp|2OVP]], [[2ovq|2OVQ]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ovr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovr OCA], [http://www.ebi.ac.uk/pdbsum/2ovr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ovr RCSB]</span> | ||
}} | }} | ||
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[[Category: Pavletich, N P.]] | [[Category: Pavletich, N P.]] | ||
[[Category: Sowa, M E.]] | [[Category: Sowa, M E.]] | ||
- | [[Category: | + | [[Category: double phosphorylation]] |
- | [[Category: f-box | + | [[Category: f-box]] |
+ | [[Category: wd40 domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:52 2008'' |
Revision as of 01:23, 31 March 2008
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, resolution 2.50Å | |||||||
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Ligands: | , | ||||||
Gene: | SKP1A, EMC19, OCP2, SKP1, TCEB1L (Homo sapiens), FBXW7, FBW7, FBX30, SEL10 (Homo sapiens) | ||||||
Related: | 2OVP, 2OVQ
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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