2jrj
From Proteopedia
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| - | [[Image:2jrj.jpg|left|200px]]<br /><applet load="2jrj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2jrj" /> | ||
| - | '''Solution structure of the human Pirh2 RING-H2 domain. Northeast Structural Genomics Consortium Target HT2B'''<br /> | ||
| - | == | + | ==Solution structure of the human Pirh2 RING-H2 domain. Northeast Structural Genomics Consortium Target HT2B== |
| - | + | <StructureSection load='2jrj' size='340' side='right'caption='[[2jrj]]' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2jrj]] 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=2JRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JRJ FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jrj OCA], [https://pdbe.org/2jrj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jrj RCSB], [https://www.ebi.ac.uk/pdbsum/2jrj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jrj ProSAT], [https://www.topsan.org/Proteins/NESGC/2jrj TOPSAN]</span></td></tr> |
| - | [ | + | </table> |
| - | [ | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/ZN363_HUMAN ZN363_HUMAN] Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity.<ref>PMID:19483087</ref> <ref>PMID:16914734</ref> <ref>PMID:18006823</ref> <ref>PMID:17721809</ref> <ref>PMID:21994467</ref> <ref>PMID:21791603</ref> <ref>PMID:19043414</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/jr/2jrj_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=2jrj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pirh2 (p53-induced RING-H2 domain protein; also known as Rchy1) is an E3 ubiquitin ligase involved in a negative-feedback loop with p53. Using NMR spectroscopy, we show that Pirh2 is a unique cysteine-rich protein comprising three modular domains. The protein binds nine zinc ions using a variety of zinc coordination schemes, including a RING domain and a left-handed beta-spiral in which three zinc ions align three consecutive small beta-sheets in an interleaved fashion. We show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. As a result, Pirh2 preferentially ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting that Pirh2 regulates protein turnover of the transcriptionally active form of p53. | ||
| - | + | Molecular basis of Pirh2-mediated p53 ubiquitylation.,Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH Nat Struct Mol Biol. 2008 Dec;15(12):1334-42. Epub 2008 Nov 30. PMID:19043414<ref>PMID:19043414</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2jrj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith CH]] | ||
| + | [[Category: Laister RC]] | ||
| + | [[Category: Lemak A]] | ||
| + | [[Category: Sheng Y]] | ||
| + | [[Category: Wu B]] | ||
Current revision
Solution structure of the human Pirh2 RING-H2 domain. Northeast Structural Genomics Consortium Target HT2B
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Laister RC | Lemak A | Sheng Y | Wu B
