3v5y
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3v5y is ON HOLD Authors: Tomchick, D.R., Bruick, R.K., Thompson, J.W., Brautigam, C.A. Description: Structure of FBXL5 hemerythrin domain, P2(1) ce...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of FBXL5 hemerythrin domain, P2(1) cell== | |
| - | + | <StructureSection load='3v5y' size='340' side='right'caption='[[3v5y]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3v5y]] is a 4 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=3V5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V5Y 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]] 2.1Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</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=3v5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v5y OCA], [https://pdbe.org/3v5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v5y RCSB], [https://www.ebi.ac.uk/pdbsum/3v5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v5y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FBXL5_HUMAN FBXL5_HUMAN] Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.<ref>PMID:17532294</ref> <ref>PMID:19762596</ref> <ref>PMID:19762597</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brautigam CA]] | ||
| + | [[Category: Bruick RK]] | ||
| + | [[Category: Thompson JW]] | ||
| + | [[Category: Tomchick DR]] | ||
Current revision
Structure of FBXL5 hemerythrin domain, P2(1) cell
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