2n9p
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of RNF126 N-terminal zinc finger domain in complex with BAG6 Ubiquitin-like domain== | |
| + | <StructureSection load='2n9p' size='340' side='right'caption='[[2n9p]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n9p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9P FirstGlance]. <br> | ||
| + | </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=2n9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9p OCA], [https://pdbe.org/2n9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9p RCSB], [https://www.ebi.ac.uk/pdbsum/2n9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RN126_HUMAN RN126_HUMAN] E3 ubiquitin-protein ligase that regulates several biological processes through ubiquitination of various target proteins. Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates. Through their polyubiquitination, may play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4. May also be part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. May provide the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the mislocalized proteins and their targeting to the proteasome (PubMed:24981174). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (PubMed:24275455). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (PubMed:23026136). May monoubiquitinate AICDA (PubMed:23277564).[UniProtKB:Q91YL2]<ref>PMID:23277564</ref> <ref>PMID:24275455</ref> <ref>PMID:24981174</ref> <ref>PMID:23026136</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sortase is also associated with SGTA, a co-chaperone from which it can obtain hydrophobic substrates. Here we solve the solution structure of the RNF126 zinc finger domain in complex with the BAG6 UBL domain. We also characterise an interaction between RNF126 and UBL4A and analyse the competition between SGTA and RNF126 for the N-terminal BAG6 binding site. This work sheds light on the sorting mechanism of the BAG6 complex and its accessory proteins which, together, decide the fate of stray hydrophobic proteins in the aqueous cytoplasm. | ||
| - | + | Structural and functional insights into the E3 ligase, RNF126.,Krysztofinska EM, Martinez-Lumbreras S, Thapaliya A, Evans NJ, High S, Isaacson RL Sci Rep. 2016 May 19;6:26433. doi: 10.1038/srep26433. PMID:27193484<ref>PMID:27193484</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2n9p" style="background-color:#fffaf0;"></div> |
| - | [[Category: Isaacson | + | |
| - | [[Category: Krysztofinska | + | ==See Also== |
| - | [[Category: Martinez-Lumbreras | + | *[[BAG family proteins 3D structures|BAG family proteins 3D structures]] |
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Isaacson RL]] | ||
| + | [[Category: Krysztofinska EM]] | ||
| + | [[Category: Martinez-Lumbreras S]] | ||
| + | [[Category: Thapaliya A]] | ||
Current revision
Solution structure of RNF126 N-terminal zinc finger domain in complex with BAG6 Ubiquitin-like domain
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