Histone deacetylase
From Proteopedia
(Difference between revisions)
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*'''HDAC class III''' | *'''HDAC class III''' | ||
| + | *SIRT1 | ||
| + | |||
| + | **[[4ig9]] – hSIRT1 + Zn<br /> | ||
| + | **[[4i5i]] – hSIRT1 + NAD + indole + Zn<br /> | ||
| + | **[[4if6]], [[4kxq]] – hSIRT1 + ADP-ribose + Zn<br /> | ||
| + | **[[5btr]] – hSIRT1 + acetyl lysine peptide + resveratol + Zn<br /> | ||
| + | **[[4zzh]] – hSIRT1 + activator + Zn<br /> | ||
| + | **[[4zzi]] – hSIRT1 + activator + inhibitor + Zn<br /> | ||
| + | **[[4zzj]] – hSIRT1 + acetyl lysine peptide + activator + Zn<br /> | ||
*SIRT2 | *SIRT2 | ||
| - | **[[2hjh]] – ySIRT2 + pseudosubstrate + nicotinamide | + | **[[2hjh]] – ySIRT2 + pseudosubstrate + nicotinamide + Zn – yeast<br /> |
| - | **[[4iao]] – ySIRT2 + SIRT4 + | + | **[[4iao]] – ySIRT2 + SIRT4 + ADP-ribose + Zn<br /> |
| + | **[[1j8f]], [[3zgo]] – hSIRT2 + Zn<br /> | ||
| + | **[[3zgv]], [[5d7o]] – hSIRT2+ ADP ribose + Zn<br /> | ||
| + | **[[4y6q]] – hSIRT2+ ADP ribose derivative + Zn<br /> | ||
| + | **[[4l3o]], [[4y6l]], [[4y6o]] – hSIRT2 + acetyl lysine peptide + Zn<br /> | ||
| + | **[[4x3o]], [[4x3p]] – hSIRT2 + myristoyl peptide + Zn<br /> | ||
| + | **[[4rmg]], [[5dy4]], [[5dy5]] – hSIRT2 + inhibitor + Zn<br /> | ||
| + | **[[5d7p]], [[5d7q]] – hSIRT2 + inhibitor + ADP-ribose + Zn<br /> | ||
| + | **[[4rmh]], [[4rmi]] – hSIRT2 + acetyl lysine peptide + inhibitor + Zn<br /> | ||
| + | **[[4r8m]] – hSIRT2 + peptide + tridecanethial + Zn<br /> | ||
| + | **[[4rmj]] – hSIRT2 + ADP-ribose + nicotinamide + Zn <br /> | ||
| + | |||
| + | *SIRT3 | ||
| + | |||
| + | **[[5d7n]] – hSIRT3 + Zn<br /> | ||
| + | **[[3gls]] – hSIRT3 (mutant) + Zn<br /> | ||
| + | **[[3glu]] – hSIRT3 + peptide + Zn<br /> | ||
| + | **[[3glr]], [[3glt]], [[4fvt]], [[4bve]], [[4v1c]] – hSIRT3 + acetyl lysine peptide + Zn<br /> | ||
| + | **[[4hd8]] – hSIRT3 + acetyl lysine peptide + piceatannol + Zn<br /> | ||
| + | **[[4fz3]] – hSIRT3 + acetyl lysine peptide + coumarine derivative + Zn<br /> | ||
| + | **[[4c78]], [[4c7b]] – hSIRT3 + acetyl lysine peptide + resveratol derivative + Zn<br /> | ||
| + | **[[4jsr]], [[4jt8]], [[4jt9]], [[4o8z]] – hSIRT3 + inhibitor + Zn<br /> | ||
| + | **[[4gbn5]] – hSIRT3 + inhibitor + carba-NAD + Zn<br/ > | ||
| + | **[[4bv3]] – hSIRT3 + inhibitor + NAD + ADP-ribose + Zn<br /> | ||
| + | **[[4bvb]], [[4bvh]] – hSIRT3 + inhibitor + ADP-ribose + Zn<br /> | ||
| + | **[[4bvf]], [[4bvg]] – hSIRT3 + acetyl lysine peptide + inhibitor + Zn<br /> | ||
| + | |||
| + | *SIRT5 | ||
| + | |||
| + | **[[2b4y]], [[4bn4]] – hSIRT5 + ADP-ribose + Zn<br /> | ||
| + | **[[2nyr]] – hSIRT5 + suramine + Zn<br /> | ||
| + | |||
| + | **[[3rig]], [[3riy]], [[4f4u]] – hSIRT5 + acetyl lysine peptide + Zn<br /> | ||
| + | **[[4gic]] – hSIRT5 + acetyl lysine peptide + carba-NAD + Zn<br/ > | ||
| + | **[[4f56]] – hSIRT5 + peptide + intermediate + Zn<br /> | ||
| + | **[[4hda]] – hSIRT5 + acetyl lysine peptide + resveratrol + Zn<br /> | ||
| + | **[[4utn]], [[4utr]], [[4utv]], [[4utx]], [[4utz]], [[4uu7]], [[4uu8]], [[4uua]], [[4uub]] – SIRT5 + acetyl lysine peptide + inhibitor + Zn - zebrafish<br /> | ||
| + | |||
| + | |||
| + | *SIRT6 | ||
| + | |||
| + | **[[3k35]] – hSIRT6 + ADP-ribose + Zn<br /> | ||
| + | **[[3pki]], [[3pkj]] – hSIRT6 (mutant) + ADP-ribose derivative + Zn<br /> | ||
| + | **[[3zg6]] – hSIRT6 + acetyl lysine peptide + ADP-ribose + Zn<br /> | ||
| + | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:31, 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
