4fo9

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==Crystal structure of the E3 SUMO Ligase PIAS2==
==Crystal structure of the E3 SUMO Ligase PIAS2==
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<StructureSection load='4fo9' size='340' side='right' caption='[[4fo9]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
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<StructureSection load='4fo9' size='340' side='right'caption='[[4fo9]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fo9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FO9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fo9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FO9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIAS2, PIASX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fo9 OCA], [https://pdbe.org/4fo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fo9 RCSB], [https://www.ebi.ac.uk/pdbsum/4fo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fo9 ProSAT]</span></td></tr>
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<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=4fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fo9 OCA], [http://pdbe.org/4fo9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/4fo9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fo9 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PIAS2_HUMAN PIAS2_HUMAN]] Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha.<ref>PMID:15920481</ref> <ref>PMID:15976810</ref>
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[https://www.uniprot.org/uniprot/PIAS2_HUMAN PIAS2_HUMAN] Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha.<ref>PMID:15920481</ref> <ref>PMID:15976810</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H]]
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[[Category: Large Structures]]
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[[Category: Bountra, C]]
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[[Category: Arrowsmith CH]]
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[[Category: Dobrovetsky, E]]
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[[Category: Bountra C]]
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[[Category: Dong, A]]
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[[Category: Dobrovetsky E]]
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[[Category: Edwards, A M]]
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[[Category: Dong A]]
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[[Category: Hu, J]]
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[[Category: Edwards AM]]
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[[Category: Structural genomic]]
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[[Category: Hu J]]
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[[Category: Tempel, W]]
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[[Category: Tempel W]]
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[[Category: Tong, Y]]
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[[Category: Tong Y]]
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[[Category: E3 ligase]]
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[[Category: Ligase]]
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[[Category: Pinit domain]]
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[[Category: Sgc]]
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[[Category: Sp-ring domain]]
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[[Category: Sumo]]
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Revision as of 20:03, 19 October 2022

Crystal structure of the E3 SUMO Ligase PIAS2

PDB ID 4fo9

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