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]] }} | ||
| - | '''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. For additional details see<br /> | + | '''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 /> |
* [[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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===HDAC class I=== | ===HDAC class I=== | ||
| + | |||
| + | ''HDAC1'' | ||
| + | |||
| + | [[4bkx]] – hHDAC1 + MTA1 – human<br /> | ||
| + | [[3hgq]], [[3hgt]] – hHDAC1 subunit 3<br /> | ||
''HDAC2'' | ''HDAC2'' | ||
| - | [[3max]] – hHDAC2 + amide derivative – | + | [[3max]] – hHDAC2 + amide derivative <br /> |
| + | [[4lxz]] – hHDAC2 core domain + SAHA<br /> | ||
| + | [[4ly1]] – hHDAC2 core domain + inhibitor<br /> | ||
''HDAC3'' | ''HDAC3'' | ||
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[[3sff]], [[3sfh]] – hHDAC8 + inhibitor<br /> | [[3sff]], [[3sfh]] – hHDAC8 + inhibitor<br /> | ||
[[1t64]], [[3f0r]] – hHDAC8 + trichostatin A <br /> | [[1t64]], [[3f0r]] – hHDAC8 + trichostatin A <br /> | ||
| - | [[1t67]], [[1w22 | + | [[1t67]], [[1w22]], [[1vkg]], [[3f07]] - hHDAC8 + amide derivative<br /> |
| + | [[1t69]] - hHDAC8 + SAHA<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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[[2v5w]] – hHDAC8 + tripeptide<br /> | [[2v5w]] – hHDAC8 + tripeptide<br /> | ||
[[3ewf]] - hHDAC8 (mutant) + polypeptide<br /> | [[3ewf]] - hHDAC8 (mutant) + polypeptide<br /> | ||
| - | [[3rqd]] - hHDAC8 + largazole | + | [[3rqd]] - hHDAC8 + largazole<br /> |
| + | [[4bz5]] – SmHDAC8 – ''Schistosoma mansoni''<br /> | ||
| + | [[4bz7]], [[4bz8]], [[4bz9]] – SmHDAC8 + inhibitor<br /> | ||
| + | [[4bz6]] – SmHDAC8 + SAHA<br /> | ||
===HDAC class IIA=== | ===HDAC class IIA=== | ||
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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]] – hHDAC4 catalytic domain + inhibitor<br /> | + | [[2vqj]], [[2vqm]], [[4cbt]] – hHDAC4 catalytic domain + inhibitor<br /> |
| - | [[2vqo]], [[2vqq]], [[2vqv]] – hHDAC4 catalytic domain (mutant) + inhibitor | + | [[2vqo]], [[2vqq]], [[2vqv]], [[4cby]] – hHDAC4 catalytic domain (mutant) + inhibitor |
''HDAC7'' | ''HDAC7'' | ||
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[[3c0y]] – hHDAC7 catalytic domain<br /> | [[3c0y]] – hHDAC7 catalytic domain<br /> | ||
[[3c0z]] - hHDAC7 catalytic domain + octanedioic acid hydroxyamide phenylamide<br /> | [[3c0z]] - hHDAC7 catalytic domain + octanedioic acid hydroxyamide phenylamide<br /> | ||
| - | [[3c10]] - hHDAC7 catalytic domain + trichostatin A | + | [[3c10]] - hHDAC7 catalytic domain + trichostatin A<br /> |
| + | [[3znr]], [[3zns]] - hHDAC7 catalytic domain + inhibitor<br /> | ||
''HDAC9'' | ''HDAC9'' | ||
| - | [[1tqe]] – | + | [[1tqe]] – mHDAC9 + myocyte-specific enhancer factor + DNA – mouse |
| - | '' | + | ''HDAC'' |
| - | [[ | + | [[4a6q]], [[4a90]] - hHDAC subunit SAP18 <br /> |
| + | [[2hde]] – hHDAC subunit SAP18 (mutant) – NMR<br /> | ||
| + | [[4a8x]] - hHDAC subunit SAP18 + RNA-binding protein + hook-like<br /> | ||
| + | [[2kdp]] – hHDAC subunit SAP30 – NMR<br /> | ||
| + | [[2ld7]] – hHDAC subunit SAP30 +SIN3A PAH 3 domain – NMR<br /> | ||
===HDAC class IIB=== | ===HDAC class IIB=== | ||
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''Sir2'' | ''Sir2'' | ||
| - | [[2hjh]] – | + | [[2hjh]] – yHDAC Sir2 - yeast<br /> |
| - | + | [[4iao]] – yHDAC Sir2 + Sir4<br /> | |
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:27, 17 March 2014
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
- Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure
- Transcription and RNA Processing.
Contents |
3D Structures of histone deacetylase
Updated on 17-March-2014
HDAC class I
HDAC1
4bkx – hHDAC1 + MTA1 – human
3hgq, 3hgt – hHDAC1 subunit 3
HDAC2
3max – hHDAC2 + amide derivative
4lxz – hHDAC2 core domain + SAHA
4ly1 – hHDAC2 core domain + inhibitor
HDAC3
4a69 – hHDAC3 + nuclear receptor corepressor 2 + inositol tetraphosphate
HDAC8
3ew8, 3ezp, 3ezt, 3f06 – hHDAC8 (mutant)
3sff, 3sfh – hHDAC8 + inhibitor
1t64, 3f0r – hHDAC8 + trichostatin A
1t67, 1w22, 1vkg, 3f07 - hHDAC8 + amide derivative
1t69 - hHDAC8 + SAHA
3mz3 - hHDAC8 (Co) + amide derivative
3mz7 - hHDAC8 (Co) (mutant) + amide derivative
3mz4 - hHDAC8 (Mn) (mutant) + amide derivative
3mz6 - hHDAC8 (Fe) (mutant) + amide derivative
2v5x - hHDAC8 (mutant) + octanediamide derivative
2v5w – hHDAC8 + tripeptide
3ewf - hHDAC8 (mutant) + polypeptide
3rqd - hHDAC8 + largazole
4bz5 – SmHDAC8 – Schistosoma mansoni
4bz7, 4bz8, 4bz9 – SmHDAC8 + inhibitor
4bz6 – SmHDAC8 + SAHA
HDAC class IIA
HDAC4
2h8n – hHDAC4 N terminal
2o94 - hHDAC4 N terminal (mutant)
2vqw - hHDAC4 catalytic domain (mutant)
2vqj, 2vqm, 4cbt – hHDAC4 catalytic domain + inhibitor
2vqo, 2vqq, 2vqv, 4cby – hHDAC4 catalytic domain (mutant) + inhibitor
HDAC7
3c0y – hHDAC7 catalytic domain
3c0z - hHDAC7 catalytic domain + octanedioic acid hydroxyamide phenylamide
3c10 - hHDAC7 catalytic domain + trichostatin A
3znr, 3zns - hHDAC7 catalytic domain + inhibitor
HDAC9
1tqe – mHDAC9 + myocyte-specific enhancer factor + DNA – mouse
HDAC
4a6q, 4a90 - hHDAC subunit SAP18
2hde – hHDAC subunit SAP18 (mutant) – NMR
4a8x - hHDAC subunit SAP18 + RNA-binding protein + hook-like
2kdp – hHDAC subunit SAP30 – NMR
2ld7 – hHDAC subunit SAP30 +SIN3A PAH 3 domain – NMR
HDAC class IIB
HDAC6
3c5k – hHDAC6 zinc finger domain
3gv4 - hHDAC6 zinc finger domain + ubiquitin peptide
3phd - hHDAC6 + polyubiquitin
HDAC class III
Sir2
2hjh – yHDAC Sir2 - yeast
4iao – yHDAC Sir2 + Sir4
