2kiz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: '''Unreleased structure''' The entry 2kiz is ON HOLD Authors: Kandias, N.G., Chasapis, C.T., Bentrop, D., Episkopou, V., Spyroulias, G.A. Description: Solution structure of Arkadia RIN...
 
OCA (talk | contribs)
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 2kiz is ON HOLD
==Solution structure of Arkadia RING-H2 finger domain==
<StructureSection load='2kiz' size='340' side='right'caption='[[2kiz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kiz]] is a 1 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 31 models</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=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/initialview03.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.


Authors: Kandias, N.G., Chasapis, C.T., Bentrop, D., Episkopou, V., Spyroulias, G.A.
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>


Description: Solution structure of Arkadia RING-H2 finger domain
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kiz" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 20 16:11:45 2009''
==See Also==
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bentrop D]]
[[Category: Chasapis CT]]
[[Category: Episkopou V]]
[[Category: Kandias NG]]
[[Category: Spyroulias GA]]