Histone deacetylase
From Proteopedia
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{{STRUCTURE_3ewf| PDB=3ewf | SIZE=400| SCENE= |right|CAPTION=Human HDAC8 tetramer complex with polypeptide, amino-methylcoumarine, K+ (purple) and Zn+2 (grey) ions, [[3ewf]] }} | {{STRUCTURE_3ewf| PDB=3ewf | SIZE=400| SCENE= |right|CAPTION=Human HDAC8 tetramer complex with polypeptide, amino-methylcoumarine, K+ (purple) and Zn+2 (grey) ions, [[3ewf]] }} | ||
| - | + | == Function == | |
| - | '''Histone deacetylase''' (HDAC) catalyzes the removal of acetyl group from ε-N-acetyl lysine in histones<ref>PMID: | + | '''Histone deacetylase''' (HDAC) catalyzes the removal of acetyl group from ε-N-acetyl lysine in histones<ref>PMID:23752268</ref>. HDAC contains Zn. DNA expression is regulated by acetylation and de-acetylation. HDAC are classified according to their domain organization to 4 classes. SAHA is a common inhibitor of HDAC. For additional details see<br /> |
* [[Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure]]<br /> | * [[Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure]]<br /> | ||
* [[Transcription and RNA Processing]]. | * [[Transcription and RNA Processing]]. | ||
| + | |||
| + | == Relevance == | ||
| + | HDAC inhibitors are used in cancer therapy<ref>PMID:11902574</ref>. | ||
== 3D Structures of histone deacetylase == | == 3D Structures of histone deacetylase == | ||
Revision as of 08:45, 23 March 2016
Contents |
Function
Histone deacetylase (HDAC) catalyzes the removal of acetyl group from ε-N-acetyl lysine in histones[1]. HDAC contains Zn. DNA expression is regulated by acetylation and de-acetylation. HDAC are classified according to their domain organization to 4 classes. SAHA is a common inhibitor of HDAC. For additional details see
- Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure
- Transcription and RNA Processing.
Relevance
HDAC inhibitors are used in cancer therapy[2].
3D Structures of histone deacetylase
Updated on 23-March-2016
References
- ↑ Joshi P, Greco TM, Guise AJ, Luo Y, Yu F, Nesvizhskii AI, Cristea IM. The functional interactome landscape of the human histone deacetylase family. Mol Syst Biol. 2013;9:672. doi: 10.1038/msb.2013.26. PMID:23752268 doi:http://dx.doi.org/10.1038/msb.2013.26
- ↑ Marks P, Rifkind RA, Richon VM, Breslow R, Miller T, Kelly WK. Histone deacetylases and cancer: causes and therapies. Nat Rev Cancer. 2001 Dec;1(3):194-202. PMID:11902574 doi:http://dx.doi.org/10.1038/35106079
