2kiz
From Proteopedia
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| - | [[  | + | ==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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KIZ FirstGlance]. <br>  | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kiz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kiz RCSB], [http://www.ebi.ac.uk/pdbsum/2kiz PDBsum]</span></td></tr>  | ||
| + | </table>  | ||
| + | == 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/chain_selection.php?pdb_ID=2ata 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>  | ||
| - | + | ==See Also==  | |
| - | + | *[[Ubiquitin protein ligase|Ubiquitin protein ligase]]  | |
| - | ==  | + | == References ==  | 
| - | [[  | + | <references/>  | 
| - | + | __TOC__  | |
| - | ==  | + | </StructureSection>  | 
| - | <  | + | [[Category: Human]]  | 
| - | [[Category:   | + | |
[[Category: Bentrop, D.]]  | [[Category: Bentrop, D.]]  | ||
[[Category: Chasapis, C T.]]  | [[Category: Chasapis, C T.]]  | ||
Revision as of 15:32, 12 October 2014
Solution structure of Arkadia RING-H2 finger domain
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