3c10
From Proteopedia
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==Crystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with Trichostatin A (TSA)== | ==Crystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with Trichostatin A (TSA)== | ||
| - | <StructureSection load='3c10' size='340' side='right' caption='[[3c10]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3c10' size='340' side='right'caption='[[3c10]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3c10]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3c10]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pqp 2pqp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C10 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TSN:TRICHOSTATIN+A'>TSN</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=3c10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c10 OCA], [https://pdbe.org/3c10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c10 RCSB], [https://www.ebi.ac.uk/pdbsum/3c10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c10 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/HDAC7_HUMAN HDAC7_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). 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. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene.<ref>PMID:12239305</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/3c10_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/3c10_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3c10 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3c10" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Histone deacetylase|Histone deacetylase]] | + | *[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Arrowsmith | + | [[Category: Large Structures]] |
| - | [[Category: Bochkarev | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Edwards | + | [[Category: Bochkarev A]] |
| - | [[Category: Loppnau | + | [[Category: Edwards AM]] |
| - | [[Category: Min | + | [[Category: Loppnau P]] |
| - | [[Category: Plotnikov | + | [[Category: Min J]] |
| - | + | [[Category: Plotnikov AN]] | |
| - | [[Category: Schuetz | + | [[Category: Schuetz A]] |
| - | [[Category: Sundstrom | + | [[Category: Sundstrom M]] |
| - | [[Category: Weigelt | + | [[Category: Weigelt J]] |
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Current revision
Crystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with Trichostatin A (TSA)
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bochkarev A | Edwards AM | Loppnau P | Min J | Plotnikov AN | Schuetz A | Sundstrom M | Weigelt J
