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2kiz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of Arkadia RING-H2 finger domain== | |
| + | <StructureSection load='2kiz' size='340' side='right'caption='[[2kiz]], [[NMR_Ensembles_of_Models | 31 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2kiz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIZ 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNF111 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2kiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kiz OCA], [https://pdbe.org/2kiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kiz RCSB], [https://www.ebi.ac.uk/pdbsum/2kiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kiz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/RN111_HUMAN RN111_HUMAN]] Acts in the NODAL pathway of mesoderm patterning during embryonic development. Acts downstream AXIN1 as an E3 ubiquitin-protein ligase which promotes the ubiquitination of inhibitory SMADs such as SMAD7, induces their proteasomal degradation and thereby enhances the transcriptional activity of TGF-beta and BMP. Activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Associates with UBE2D2 as an E2 enzyme.<ref>PMID:14657019</ref> <ref>PMID:16601693</ref> <ref>PMID:17591695</ref> <ref>PMID:22411132</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ki/2kiz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kiz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Arkadia (Rnf111), an E3 Ubiquitin (Ub) ligase, amplifies TGF-beta signaling responses by targeting for degradation of the negative regulators Smad6/7 and the SnoN/Ski transcriptional repressors when they block the TGF-beta effectors Smad2/3. The E3 ligase activity of Arkadia depends on its C-terminal RING-H2 domain that constitutes the docking site for the E2 Ub-conjugating enzyme carrying the activated Ub. We determined the nuclear magnetic resonance solution structure of Arkadia's RING-H2 domain and revealed a (beta)betabetaalpha fold, fully consistent with the expected "cross-brace" mode of Zn(II)-ligation. In addition, the interaction of the Arkadia RING-H2 domain with its E2 partner enzyme (UbcH5b) was examined through chemical shift perturbation. Proteins 2012. (c) 2012 Wiley Periodicals, Inc. | ||
| - | + | NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase.,Chasapis CT, Kandias NG, Episkopou V, Bentrop D, Spyroulias GA Proteins. 2012 May;80(5):1484-9. doi: 10.1002/prot.24048. Epub 2012 Mar 13. PMID:22411132<ref>PMID:22411132</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2kiz" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bentrop, D]] | ||
| + | [[Category: Chasapis, C T]] | ||
| + | [[Category: Episkopou, V]] | ||
| + | [[Category: Kandias, N G]] | ||
| + | [[Category: Spyroulias, G A]] | ||
| + | [[Category: Arkadia]] | ||
| + | [[Category: E3 ligase]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Ring-h2 finger]] | ||
| + | [[Category: Zinc-finger]] | ||
| + | [[Category: Zn binding domain]] | ||
Current revision
Solution structure of Arkadia RING-H2 finger domain
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