3v5y: Difference between revisions

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==Structure of FBXL5 hemerythrin domain, P2(1) cell==
==Structure of FBXL5 hemerythrin domain, P2(1) cell==
<StructureSection load='3v5y' size='340' side='right' caption='[[3v5y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3v5y' size='340' side='right'caption='[[3v5y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v5y]] is a 4 chain structure with sequence 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=3V5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V5Y FirstGlance]. <br>
<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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene><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]] 2.1&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v5x|3v5x]], [[3v5z|3v5z]]</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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBL4, FBL5, FBXL5, FLR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v5y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v5y RCSB], [http://www.ebi.ac.uk/pdbsum/3v5y PDBsum]</span></td></tr>
</table>
<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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Structural and molecular characterization of the iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5).,Thompson JW, Salahudeen AA, Chollangi S, Ruiz JC, Brautigam CA, Makris TM, Lipscomb JD, Tomchick DR, Bruick RK J Biol Chem. 2012 Jan 17. PMID:22253436<ref>PMID:22253436</ref>
Structural and molecular characterization of the iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5).,Thompson JW, Salahudeen AA, Chollangi S, Ruiz JC, Brautigam CA, Makris TM, Lipscomb JD, Tomchick DR, Bruick RK J Biol Chem. 2012 Jan 17. PMID:22253436<ref>PMID:22253436</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3v5y" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Brautigam, C A.]]
[[Category: Large Structures]]
[[Category: Bruick, R K.]]
[[Category: Brautigam CA]]
[[Category: Thompson, J W.]]
[[Category: Bruick RK]]
[[Category: Tomchick, D R.]]
[[Category: Thompson JW]]
[[Category: Alpha helical bundle]]
[[Category: Tomchick DR]]
[[Category: E3 ubiquitin ligase complex]]
[[Category: Gene regulation]]
[[Category: Hemerythrin]]
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