5d1c: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of D233G-Y306F HDAC8 in complex with a tetrapeptide substrate==
 
<StructureSection load='5d1c' size='340' side='right' caption='[[5d1c]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
The entry 5d1c is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5d1c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D1C FirstGlance]. <br>
Authors: Decroos, C., Christianson, N.H., Gullett, L.E., Bowman, C.M., Christianson, K.E., Deardorff, M.A., Christianson, D.W.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=MCM:7-AMINO-4-METHYL-CHROMEN-2-ONE'>MCM</scene></td></tr>
Description: Crystal structure of D233G-Y306F HDAC8 in complex with a tetrapeptide substrate
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d1b|5d1b]], [[5d1d|5d1d]]</td></tr>
[[Category: Unreleased Structures]]
<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>
[[Category: Christianson, K.E]]
<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=5d1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d1c OCA], [http://pdbe.org/5d1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d1c RCSB], [http://www.ebi.ac.uk/pdbsum/5d1c PDBsum]</span></td></tr>
</table>
== Function ==
[[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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Histone deacetylase]]
[[Category: Bowman, C M]]
[[Category: Christianson, D W]]
[[Category: Christianson, K E]]
[[Category: Christianson, N H]]
[[Category: Deardorff, M A]]
[[Category: Decroos, C]]
[[Category: Decroos, C]]
[[Category: Deardorff, M.A]]
[[Category: Gullett, L E]]
[[Category: Bowman, C.M]]
[[Category: Arginase/deacetylase fold]]
[[Category: Christianson, D.W]]
[[Category: Enzyme substrate complex]]
[[Category: Gullett, L.E]]
[[Category: Hydrolase]]
[[Category: Christianson, N.H]]

Revision as of 08:33, 22 October 2015

Crystal structure of D233G-Y306F HDAC8 in complex with a tetrapeptide substrateCrystal structure of D233G-Y306F HDAC8 in complex with a tetrapeptide substrate

Structural highlights

5d1c is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
NonStd Res:, ,
Activity:Histone deacetylase, with EC number 3.5.1.98
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.[1] [2] [3] [4]

References

  1. ↑ Hu E, Chen Z, Fredrickson T, Zhu Y, Kirkpatrick R, Zhang GF, Johanson K, Sung CM, Liu R, Winkler J. Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. J Biol Chem. 2000 May 19;275(20):15254-64. PMID:10748112 doi:http://dx.doi.org/10.1074/jbc.M908988199
  2. ↑ Buggy JJ, Sideris ML, Mak P, Lorimer DD, McIntosh B, Clark JM. Cloning and characterization of a novel human histone deacetylase, HDAC8. Biochem J. 2000 Aug 15;350 Pt 1:199-205. PMID:10926844
  3. ↑ Van den Wyngaert I, de Vries W, Kremer A, Neefs J, Verhasselt P, Luyten WH, Kass SU. Cloning and characterization of human histone deacetylase 8. FEBS Lett. 2000 Jul 28;478(1-2):77-83. PMID:10922473
  4. ↑ Lee H, Rezai-Zadeh N, Seto E. Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. Mol Cell Biol. 2004 Jan;24(2):765-73. PMID:14701748

5d1c, resolution 1.42Å

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