2l00: Difference between revisions
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==Solution structure of the non-covalent complex of the ZNF216 A20 domain with ubiquitin== | ==Solution structure of the non-covalent complex of the ZNF216 A20 domain with ubiquitin== | ||
<StructureSection load='2l00' size='340' side='right' caption='[[2l00 | <StructureSection load='2l00' size='340' side='right'caption='[[2l00]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2l00]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2l00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L00 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <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=2l00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l00 OCA], [https://pdbe.org/2l00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l00 RCSB], [https://www.ebi.ac.uk/pdbsum/2l00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l00 ProSAT]</span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/ZFAN5_RAT ZFAN5_RAT] Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation (By similarity). | |||
==See Also== | ==See Also== | ||
*[[ | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Garner | [[Category: Garner TP]] | ||
[[Category: Layfield | [[Category: Layfield R]] | ||
[[Category: Long | [[Category: Long JE]] | ||
[[Category: Searle | [[Category: Searle MS]] | ||
Latest revision as of 06:50, 1 May 2024
Solution structure of the non-covalent complex of the ZNF216 A20 domain with ubiquitin
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