Histone deacetylase
From Proteopedia
(Difference between revisions)
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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 == | == Function == | ||
| - | '''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 | + | '''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. SAHA is a common inhibitor of HDAC. HDAC are classified according to their domain organization into 4 classes. <br /> |
| + | * '''HDAC class I''' are homologous to yeast Rpd3.<br /> | ||
| + | * '''HDAC class II''' are homologous to yeast HdaI.<br /> | ||
| + | * '''HDAC class III''' called '''sirtuin''' - Silent Information Regulator) (SIRT) are NAD-dependent HDAC <ref>PMID:18249170</ref>.<br /> | ||
| + | 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 == | == Relevance == | ||
| - | HDAC inhibitors are used in cancer therapy<ref>PMID:11902574</ref>. | + | HDAC inhibitors are used in cancer therapy<ref>PMID:11902574</ref>. Sirtuins play a role in cancer, metabolic activity and neurodegenerative diseases<ref>PMID:17456799</ref>. |
== 3D Structures of histone deacetylase == | == 3D Structures of histone deacetylase == | ||
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*'''HDAC class III''' | *'''HDAC class III''' | ||
| - | * | + | *SIRT2 |
| - | **[[2hjh]] – | + | **[[2hjh]] – ySIRT2 + pseudosubstrate + nicotinamide - yeast<br /> |
| - | **[[4iao]] – | + | **[[4iao]] – ySIRT2 + SIRT4 + adenosine diphosphoribose<br /> |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:49, 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. SAHA is a common inhibitor of HDAC. HDAC are classified according to their domain organization into 4 classes.
- HDAC class I are homologous to yeast Rpd3.
- HDAC class II are homologous to yeast HdaI.
- HDAC class III called sirtuin - Silent Information Regulator) (SIRT) are NAD-dependent HDAC [2].
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[3]. Sirtuins play a role in cancer, metabolic activity and neurodegenerative diseases[4].
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
- ↑ Schwer B, Verdin E. Conserved metabolic regulatory functions of sirtuins. Cell Metab. 2008 Feb;7(2):104-12. doi: 10.1016/j.cmet.2007.11.006. PMID:18249170 doi:http://dx.doi.org/10.1016/j.cmet.2007.11.006
- ↑ 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
- ↑ Yamamoto H, Schoonjans K, Auwerx J. Sirtuin functions in health and disease. Mol Endocrinol. 2007 Aug;21(8):1745-55. Epub 2007 Apr 24. PMID:17456799 doi:http://dx.doi.org/10.1210/me.2007-0079
