4a69
From Proteopedia
(Difference between revisions)
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<StructureSection load='4a69' size='340' side='right'caption='[[4a69]], [[Resolution|resolution]] 2.06Å' scene=''> | <StructureSection load='4a69' size='340' side='right'caption='[[4a69]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4a69]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4a69]] is a 4 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=4A69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A69 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=I0P:D-MYO+INOSITOL+1,4,5,6+TETRAKISPHOSPHATE'>I0P</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=I0P:D-MYO+INOSITOL+1,4,5,6+TETRAKISPHOSPHATE'>I0P</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <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=4a69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a69 OCA], [https://pdbe.org/4a69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a69 RCSB], [https://www.ebi.ac.uk/pdbsum/4a69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a69 ProSAT]</span></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=4a69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a69 OCA], [https://pdbe.org/4a69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a69 RCSB], [https://www.ebi.ac.uk/pdbsum/4a69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a69 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/HDAC3_HUMAN HDAC3_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:21444723, PubMed:23911289). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803).<ref>PMID:21444723</ref> <ref>PMID:23911289</ref> <ref>PMID:25190803</ref> | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Fairall | + | [[Category: Fairall L]] |
- | [[Category: Santos | + | [[Category: Santos GM]] |
- | [[Category: Schwabe | + | [[Category: Schwabe JWR]] |
- | [[Category: Watson | + | [[Category: Watson PJ]] |
- | + | ||
- | + |
Current revision
Structure of HDAC3 bound to corepressor and inositol tetraphosphate
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