5thv

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'''Unreleased structure'''
 
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The entry 5thv is ON HOLD until Paper Publication
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==Crystal Structure of G305A HDAC8 in complex with M344==
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<StructureSection load='5thv' size='340' side='right' caption='[[5thv]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
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Authors: Porter, N.J., Christianson, D.W.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5thv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5THV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5THV FirstGlance]. <br>
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Description: Crystal Structure of G305A HDAC8 in complex with M344
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B3N:4-(DIMETHYLAMINO)-N-[7-(HYDROXYAMINO)-7-OXOHEPTYL]BENZAMIDE'>B3N</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ths|5ths]], [[5tht|5tht]], [[5thu|5thu]]</td></tr>
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[[Category: Porter, N.J]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>
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[[Category: Christianson, D.W]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5thv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5thv OCA], [http://pdbe.org/5thv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5thv RCSB], [http://www.ebi.ac.uk/pdbsum/5thv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5thv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Histone deacetylase]]
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[[Category: Christianson, D W]]
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[[Category: Porter, N J]]
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[[Category: Hydrolase]]
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[[Category: Zinc histone deactylase]]

Revision as of 21:46, 22 December 2016

Crystal Structure of G305A HDAC8 in complex with M344

5thv, resolution 1.87Å

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