3c10: Difference between revisions

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<StructureSection load='3c10' size='340' side='right'caption='[[3c10]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3c10' size='340' side='right'caption='[[3c10]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3c10]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
<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='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>
</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&#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;'>[[2nvr|2nvr]], [[3c0y|3c0y]], [[3c0z|3c0z]]</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=TSN:TRICHOSTATIN+A'>TSN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDAC7A, HDAC7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[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>
</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>
[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bochkarev, A]]
[[Category: Bochkarev A]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Loppnau, P]]
[[Category: Loppnau P]]
[[Category: Min, J]]
[[Category: Min J]]
[[Category: Plotnikov, A N]]
[[Category: Plotnikov AN]]
[[Category: Structural genomic]]
[[Category: Schuetz A]]
[[Category: Schuetz, A]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Alternative splicing]]
[[Category: Chromatin regulator]]
[[Category: Cytoplasm]]
[[Category: Hdac]]
[[Category: Hydrolase]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Repressor]]
[[Category: Sgc]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
Retrieved from "https://proteopedia.org/3c10"