2vqq: Difference between revisions

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<StructureSection load='2vqq' size='340' side='right'caption='[[2vqq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2vqq' size='340' side='right'caption='[[2vqq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2vqq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2vqq]] 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=2VQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VQQ FirstGlance]. <br>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vqw|2vqw]], [[2vqo|2vqo]], [[2vqv|2vqv]], [[2vqm|2vqm]], [[2vqj|2vqj]]</div></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqq OCA], [https://pdbe.org/2vqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vqq RCSB], [https://www.ebi.ac.uk/pdbsum/2vqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqq 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=2vqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vqq OCA], [https://pdbe.org/2vqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vqq RCSB], [https://www.ebi.ac.uk/pdbsum/2vqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vqq ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[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>
== Function ==
[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bottomley, M J]]
[[Category: Bottomley MJ]]
[[Category: Carfi, A]]
[[Category: Carfi A]]
[[Category: Cirillo, A]]
[[Category: Cirillo A]]
[[Category: Ferrigno, F]]
[[Category: De Francesco R]]
[[Category: Francesco, R De]]
[[Category: Di Giovine P]]
[[Category: Gallinari, P]]
[[Category: Ferrigno F]]
[[Category: Giovine, P Di]]
[[Category: Gallinari P]]
[[Category: Jones, P]]
[[Category: Jones P]]
[[Category: Neddermann, P]]
[[Category: Lo Surdo P]]
[[Category: Scarpelli, R]]
[[Category: Neddermann P]]
[[Category: Steinkuhler, C]]
[[Category: Scarpelli R]]
[[Category: Surdo, P Lo]]
[[Category: Steinkuhler C]]
[[Category: Chromatin]]
[[Category: Chromatin regulator]]
[[Category: Coiled coil]]
[[Category: Cytoplasm]]
[[Category: Hdac]]
[[Category: Hdaci]]
[[Category: Histone deacetylase]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Repressor]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Ubl conjugation]]
[[Category: Zinc]]

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