Histone deacetylase
From Proteopedia
(Difference between revisions)
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**[[4bkx]] – hHDAC1 + MTA1 – human<br /> | **[[4bkx]] – hHDAC1 + MTA1 – human<br /> | ||
**[[3hgq]], [[3hgt]] – hHDAC1 subunit 3<br /> | **[[3hgq]], [[3hgt]] – hHDAC1 subunit 3<br /> | ||
+ | **[[5icn]] – hHDAC1 + MTA1 + peptide<br /> | ||
+ | **[[5j8j]] – yHDAC1 residues 457-698 – yeast<br /> | ||
*HDAC2 | *HDAC2 | ||
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**[[3max]] – hHDAC2 + amide derivative <br /> | **[[3max]] – hHDAC2 + amide derivative <br /> | ||
**[[4lxz]] – hHDAC2 core domain + SAHA<br /> | **[[4lxz]] – hHDAC2 core domain + SAHA<br /> | ||
- | **[[4ly1]] – hHDAC2 core domain + inhibitor<br /> | + | **[[4ly1]], [[5iwg]], [[5ix0]] – hHDAC2 core domain + inhibitor<br /> |
*HDAC3 | *HDAC3 | ||
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**[[3ew8]], [[3ezp]], [[3ezt]], [[3f06]] – hHDAC8 (mutant)<br /> | **[[3ew8]], [[3ezp]], [[3ezt]], [[3f06]] – hHDAC8 (mutant)<br /> | ||
**[[3sff]], [[3sfh]] – hHDAC8 + inhibitor<br /> | **[[3sff]], [[3sfh]] – hHDAC8 + inhibitor<br /> | ||
- | **[[1t64]], [[3f0r]] – hHDAC8 + trichostatin A <br /> | + | **[[1t64]], [[3f0r]], [[5ths]] – hHDAC8 + trichostatin A <br /> |
+ | **[[5tht]], [[5thu]], [[5thv]], [[5dc5]], [[5d1b]] - hHDAC8 (mutant) + amide derivative<br /> | ||
**[[1t67]], [[1w22]], [[1vkg]], [[3f07]] - hHDAC8 + amide derivative<br /> | **[[1t67]], [[1w22]], [[1vkg]], [[3f07]] - hHDAC8 + amide derivative<br /> | ||
**[[1t69]] - hHDAC8 + SAHA<br /> | **[[1t69]] - hHDAC8 + SAHA<br /> | ||
**[[4qa0]] - hHDAC8 (mutant) + SAHA<br /> | **[[4qa0]] - hHDAC8 (mutant) + SAHA<br /> | ||
+ | **[[5fcw]], [[5fue]] - hHDAC8 + hydroxamate<br /> | ||
**[[4qa1]], [[4qa2]], [[4qa3]], [[4qa4]] - hHDAC8 (mutant) + inhibitor<br /> | **[[4qa1]], [[4qa2]], [[4qa3]], [[4qa4]] - hHDAC8 (mutant) + inhibitor<br /> | ||
**[[2v5w]] – hHDAC8 + tripeptide substrate<br /> | **[[2v5w]] – hHDAC8 + tripeptide substrate<br /> | ||
- | **[[4qa5]], [[4qa6]], [[4qa7]], [[3ewf]] - hHDAC8 (mutant) + tetrapeptide substrate<br /> | + | **[[4qa5]], [[4qa6]], [[4qa7]], [[3ewf]], [[5dc8]], [[5dc7]], [[5dc6]], [[5d1d]], [[5d1c]] - hHDAC8 (mutant) + tetrapeptide substrate<br /> |
**[[3rqd]] - hHDAC8 + largazole<br /> | **[[3rqd]] - hHDAC8 + largazole<br /> | ||
**[[4rn0]], [[4rn1]], [[4rn2]] - hHDAC8 (mutant) + largazole analog<br /> | **[[4rn0]], [[4rn1]], [[4rn2]] - hHDAC8 (mutant) + largazole analog<br /> | ||
+ | **[[5bwz]] - hHDAC8 (mutant) + droxinostat<br /> | ||
**[[3mz3]] - hHDAC8 (Co) + amide derivative<br /> | **[[3mz3]] - hHDAC8 (Co) + amide derivative<br /> | ||
**[[3mz7]] - hHDAC8 (Co) (mutant) + amide derivative<br /> | **[[3mz7]] - hHDAC8 (Co) (mutant) + amide derivative<br /> | ||
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**[[2o94]] - hHDAC4 N terminal (mutant)<br /> | **[[2o94]] - hHDAC4 N terminal (mutant)<br /> | ||
**[[2vqw]] - hHDAC4 catalytic domain (mutant)<br /> | **[[2vqw]] - hHDAC4 catalytic domain (mutant)<br /> | ||
- | **[[2vqj]], [[2vqm]], [[4cbt]] – hHDAC4 catalytic domain + inhibitor<br /> | + | **[[2vqj]], [[2vqm]], [[4cbt]], [[5a2s]] – hHDAC4 catalytic domain + inhibitor<br /> |
**[[2vqo]], [[2vqq]], [[2vqv]], [[4cby]] – hHDAC4 catalytic domain (mutant) + inhibitor | **[[2vqo]], [[2vqq]], [[2vqv]], [[4cby]] – hHDAC4 catalytic domain (mutant) + inhibitor | ||
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**[[2kdp]] – hHDAC subunit SAP30 – NMR<br /> | **[[2kdp]] – hHDAC subunit SAP30 – NMR<br /> | ||
**[[2ld7]] – hHDAC subunit SAP30 +SIN3A PAH 3 domain – NMR<br /> | **[[2ld7]] – hHDAC subunit SAP30 +SIN3A PAH 3 domain – NMR<br /> | ||
+ | **[[5ikk]] – HDAC CLR3 – fission yeast<br /> | ||
*'''HDAC class IIB''' | *'''HDAC class IIB''' | ||
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**[[3c5k]] – hHDAC6 zinc finger domain<br /> | **[[3c5k]] – hHDAC6 zinc finger domain<br /> | ||
**[[3gv4]] - hHDAC6 zinc finger domain + ubiquitin peptide<br /> | **[[3gv4]] - hHDAC6 zinc finger domain + ubiquitin peptide<br /> | ||
- | **[[3phd]] - hHDAC6 + polyubiquitin | + | **[[3phd]] - hHDAC6 + polyubiquitin<br /> |
+ | **[[5kh3]], [[5kh7]], [[5kh9]], [[5b8d]] – hHDAC6 zinc finger + inhibitor<br /> | ||
*'''HDAC class III''' | *'''HDAC class III''' | ||
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*SIRT2 | *SIRT2 | ||
- | **[[2hjh]] – ySIRT2 + pseudosubstrate + nicotinamide + Zn | + | **[[2hjh]] – ySIRT2 + pseudosubstrate + nicotinamide + Zn <br /> |
**[[4iao]] – ySIRT2 + SIRT4 + ADP-ribose + Zn<br /> | **[[4iao]] – ySIRT2 + SIRT4 + ADP-ribose + Zn<br /> | ||
**[[1j8f]], [[3zgo]] – hSIRT2 + Zn<br /> | **[[1j8f]], [[3zgo]] – hSIRT2 + Zn<br /> | ||
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**[[4f56]] – hSIRT5 + peptide + intermediate + Zn<br /> | **[[4f56]] – hSIRT5 + peptide + intermediate + Zn<br /> | ||
**[[4hda]] – hSIRT5 + acetyl lysine peptide + resveratrol + Zn<br /> | **[[4hda]] – hSIRT5 + acetyl lysine peptide + resveratrol + Zn<br /> | ||
- | **[[4utn]], [[4utr]], [[4utv]], [[4utx]], [[4utz]], [[4uu7]], [[4uu8]], [[4uua]], [[4uub]] – | + | **[[4utn]], [[4utr]], [[4utv]], [[4utx]], [[4utz]], [[4uu7]], [[4uu8]], [[4uua]], [[4uub]] – zeSIRT5 + acetyl lysine peptide + inhibitor + Zn - zebrafish<br /> |
Revision as of 06:20, 13 June 2017
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3D Structures of histone deacetylase
Updated on 13-June-2017
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
- ↑ Mann BS, Johnson JR, Cohen MH, Justice R, Pazdur R. FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma. Oncologist. 2007 Oct;12(10):1247-52. PMID:17962618 doi:http://dx.doi.org/10.1634/theoncologist.12-10-1247
- ↑ Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB. Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem. 2009 Sep 4;284(36):24394-405. Epub 2009 Jun 16. PMID:19535340 doi:10.1074/jbc.M109.014928