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==Crystal Structure of HDA15 HD domain== | |||
<StructureSection load='6j6t' size='340' side='right'caption='[[6j6t]], [[Resolution|resolution]] 2.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6j6t]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J6T FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><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=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
[[Category: | <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> | ||
<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=6j6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j6t OCA], [http://pdbe.org/6j6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j6t RCSB], [http://www.ebi.ac.uk/pdbsum/6j6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j6t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/HDA15_ARATH HDA15_ARATH]] 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 (By similarity). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Histone deacetylase]] | |||
[[Category: Large Structures]] | |||
[[Category: Cheng, Y S]] | |||
[[Category: Hsu, J C]] | |||
[[Category: Hung, H C]] | |||
[[Category: Liu, T C]] | |||
[[Category: Arabidopsis]] | |||
[[Category: Gene regulation]] | |||
Revision as of 19:06, 22 January 2020
Crystal Structure of HDA15 HD domainCrystal Structure of HDA15 HD domain
Structural highlights
Function[HDA15_ARATH] 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 (By similarity). |
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