2vqo

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==STRUCTURE OF HDAC4 CATALYTIC DOMAIN WITH A GAIN-OF-FUNCTION MUATION BOUND TO A TRIFLUOROMETHYLKETONE INHBITOR==
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<StructureSection load='2vqo' size='340' side='right' caption='[[2vqo]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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==Structure of HDAC4 catalytic domain with a gain-of-function muation bound to a trifluoromethylketone inhbitor==
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<StructureSection load='2vqo' size='340' side='right'caption='[[2vqo]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VQO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2vqo]] is a 2 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=2VQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQO FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TFG:2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL'>TFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vqw|2vqw]], [[2vqq|2vqq]], [[2vqv|2vqv]], [[2vqm|2vqm]], [[2vqj|2vqj]]</td></tr>
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<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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TFG:2,2,2-TRIFLUORO-1-{5-[(3-PHENYL-5,6-DIHYDROIMIDAZO[1,2-A]PYRAZIN-7(8H)-YL)CARBONYL]THIOPHEN-2-YL}ETHANE-1,1-DIOL'>TFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vqo RCSB], [http://www.ebi.ac.uk/pdbsum/2vqo PDBsum]</span></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=2vqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqo OCA], [https://pdbe.org/2vqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vqo RCSB], [https://www.ebi.ac.uk/pdbsum/2vqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqo ProSAT]</span></td></tr>
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<table>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HDAC4_HUMAN HDAC4_HUMAN] Defects in HDAC4 are the cause of brachydactyly-mental retardation syndrome (BDMR) [MIM:[https://omim.org/entry/600430 600430]. A syndrome resembling the physical anomalies found in Albright hereditary osteodystrophy. Common features are mild facial dysmorphism, congenital heart defects, distinct brachydactyly type E, mental retardation, developmental delay, seizures, autism spectrum disorder, and stocky build. Soft tissue ossification is absent, and there are no abnormalities in parathyroid hormone or calcium metabolism.<ref>PMID:20691407</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HDAC4_HUMAN HDAC4_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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D.<ref>PMID:10523670</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>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/2vqo_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/2vqo_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>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=2vqo 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2vqo" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Histone deacetylase|Histone deacetylase]]
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*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bottomley, M J.]]
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[[Category: Large Structures]]
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[[Category: Carfi, A.]]
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[[Category: Bottomley MJ]]
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[[Category: Cirillo, A.]]
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[[Category: Carfi A]]
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[[Category: Ferrigno, F.]]
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[[Category: Cirillo A]]
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[[Category: Francesco, R De.]]
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[[Category: De Francesco R]]
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[[Category: Gallinari, P.]]
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[[Category: Di Giovine P]]
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[[Category: Giovine, P Di.]]
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[[Category: Ferrigno F]]
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[[Category: Jones, P.]]
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[[Category: Gallinari P]]
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[[Category: Neddermann, P.]]
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[[Category: Jones P]]
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[[Category: Scarpelli, R.]]
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[[Category: Lo Surdo P]]
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[[Category: Steinkuhler, C.]]
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[[Category: Neddermann P]]
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[[Category: Surdo, P Lo.]]
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[[Category: Scarpelli R]]
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[[Category: Chromatin]]
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[[Category: Steinkuhler C]]
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[[Category: Chromatin regulator]]
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[[Category: Hdac]]
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[[Category: Hdaci]]
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[[Category: Histone deacetylase]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

Structure of HDAC4 catalytic domain with a gain-of-function muation bound to a trifluoromethylketone inhbitor

PDB ID 2vqo

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OCA

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