5n4w
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5n4w is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the Cul2-Rbx1-EloBC-VHL ubiquitin ligase complex== | |
| + | <StructureSection load='5n4w' size='340' side='right'caption='[[5n4w]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5n4w]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N4W FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4w OCA], [https://pdbe.org/5n4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n4w RCSB], [https://www.ebi.ac.uk/pdbsum/5n4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CUL2_HUMAN CUL2_HUMAN] Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF). | ||
| - | + | ==See Also== | |
| - | + | *[[Cullin 3D structures|Cullin 3D structures]] | |
| - | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | |
| - | [[Category: | + | *[[Ring box protein 3D structures|Ring box protein 3D structures]] |
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cardote TAF]] | ||
| + | [[Category: Ciulli A]] | ||
| + | [[Category: Gadd MS]] | ||
Current revision
Crystal structure of the Cul2-Rbx1-EloBC-VHL ubiquitin ligase complex
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