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<StructureSection load='5vmd' size='340' side='right'caption='[[5vmd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5vmd' size='340' side='right'caption='[[5vmd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5vmd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VMD FirstGlance]. <br>
<table><tr><td colspan='2'>[[5vmd]] 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=5VMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VMD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.202&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBXO11, FBX11, PRMT9, VIT1, UG063H01 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vmd OCA], [http://pdbe.org/5vmd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vmd RCSB], [http://www.ebi.ac.uk/pdbsum/5vmd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vmd ProSAT]</span></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=5vmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vmd OCA], [https://pdbe.org/5vmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vmd RCSB], [https://www.ebi.ac.uk/pdbsum/5vmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vmd ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/FBX11_HUMAN FBX11_HUMAN]] Vitiligo. Defects in FBXO11 may be a cause of diffuse large B-cell lymphoma by allowing the accumulation of BCL6, an oncoprotein that has a critical role in lymphomas.<ref>PMID:22113614</ref>
[https://www.uniprot.org/uniprot/FBX11_HUMAN FBX11_HUMAN] Vitiligo. Defects in FBXO11 may be a cause of diffuse large B-cell lymphoma by allowing the accumulation of BCL6, an oncoprotein that has a critical role in lymphomas.<ref>PMID:22113614</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FBX11_HUMAN FBX11_HUMAN]] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53.<ref>PMID:17098746</ref> <ref>PMID:22113614</ref> <ref>PMID:23478441</ref> <ref>PMID:23478445</ref> <ref>PMID:23892434</ref> <ref>PMID:24613396</ref>
[https://www.uniprot.org/uniprot/FBX11_HUMAN FBX11_HUMAN] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11) complex mediates ubiquitination and degradation of BCL6, thereby playing a role in the germinal center B-cells terminal differentiation toward memory B-cells and plasma cells. The SCF(FBXO11) complex also mediates ubiquitination and degradation of DTL, an important step for the regulation of TGF-beta signaling, cell migration and the timing of the cell-cycle progression and exit. Binds to and neddylates phosphorylated p53/TP53, inhibiting its transcriptional activity. SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53.<ref>PMID:17098746</ref> <ref>PMID:22113614</ref> <ref>PMID:23478441</ref> <ref>PMID:23478445</ref> <ref>PMID:23892434</ref> <ref>PMID:24613396</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases that directly binds N-terminal degradation signals in substrate proteins. UBR6, also called FBXO11, is an UBR-box containing E3 ubiquitin ligase that does not bind N-terminal signals. Here, we present the crystal structure of the UBR-box domain from human UBR6. The dimeric crystal structure reveals a unique form of domain swapping mediated by zinc coordination, where three independent protein chains come together to regenerate the topology of the monomeric UBR-box fold. Analysis of the structure suggests that the absence of N-terminal residue binding arises from the lack of an amino acid binding pocket.


Crystal structure of the UBR-box from UBR6/FBXO11 reveals domain swapping mediated by zinc binding.,Munoz-Escobar J, Kozlov G, Gehring K Protein Sci. 2017 Jul 10. doi: 10.1002/pro.3227. PMID:28691247<ref>PMID:28691247</ref>
==See Also==
 
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vmd" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gehring, K]]
[[Category: Gehring K]]
[[Category: Kozlov, G]]
[[Category: Kozlov G]]
[[Category: Munoz-Escobar, J]]
[[Category: Munoz-Escobar J]]
[[Category: Domain swapping]]
[[Category: Fbxo11]]
[[Category: Ligase]]
[[Category: Ubr-box]]
[[Category: Ubr6]]
[[Category: Zinc]]
[[Category: Zinc finger]]

Latest revision as of 14:11, 13 March 2024

Crystal structure of UBR-box from UBR6 in a domain-swapping conformation

5vmd, resolution 2.20Å

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