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]] }} | ||
- | '''Histone deacetylase''' (HDAC) catalyzes the removal of acetyl group from ε-N-acetyl lysine in histones. 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 /> | + | '''Histone deacetylase''' (HDAC) catalyzes the removal of acetyl group from ε-N-acetyl lysine in histones<ref>PMID:8528769</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]]. | ||
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**[[4iao]] – yHDAC Sir2 + Sir4<br /> | **[[4iao]] – yHDAC Sir2 + Sir4<br /> | ||
}} | }} | ||
+ | == References == | ||
+ | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 07:59, 23 March 2016
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.
3D Structures of histone deacetylase
Updated on 23-March-2016
References
- ↑ White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr Opin Struct Biol. 1995 Aug;5(4):521-7. PMID:8528769