Histone deacetylase

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(New page: {{STRUCTURE_3ewf| PDB=3ewf | SIZE=400| SCENE= |right|CAPTION=Human HDAC8 complex with polypeptide, 3ewf }} '''Histone deacetylase''' (HDAC) catalyzes the removal of acetyl group fr...)
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{{STRUCTURE_3ewf| PDB=3ewf | SIZE=400| SCENE= |right|CAPTION=Human HDAC8 complex with polypeptide, [[3ewf]] }}
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{{STRUCTURE_3ewf| PDB=3ewf | SIZE=400| SCENE= |right|CAPTION=Human HDAC8 complex with polypeptide, amino-methylcoumarine, K+ and Zn+2 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 [[Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure]].
'''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 [[Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure]].

Revision as of 11:59, 20 February 2012

Template:STRUCTURE 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 Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure.

Contents

3D Structures of histone deacetylase

HDAC class I

HDAC2

3max – hHDAC2 + amide derivative – human

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, 1t69, 1vkg, 3f07 - hHDAC8 + amide derivative
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

HDAC class IIA

HDAC4

2h8n – hHDAC4 N terminal
2o94 - hHDAC4 N terminal (mutant)
2vqw - hHDAC4 catalytic domain (mutant)
2vqj, 2vqm – hHDAC4 catalytic domain + inhibitor
2vqo, 2vqq, 2vqv – hHDAC4 catalytic domain (mutant) + inhibitor

HDAC7

3c0y – hHDAC7 catalytic domain
3c0z - hHDAC7 catalytic domain + octanedioic acid hydroxyamide phenylamide
3c10 - hHDAC7 catalytic domain + trichostatin A

HDAC9

1tqe – HDAC9 + myocyte-specific enhancer factor + DNA – mouse

HDA1

3hgq, 3hgt – Hda1 subunit 3

HDAC class IIB

HDAC6

3c5k – hHDAC6 zinc finger domain
3gv4 - hHDAC6 zinc finger domain + ubiquitin peptide
3phd - hHDAC6 + polyubiquitin

HDAC class III

Sir2

2hjh – HDAC Sir2]] - yeast

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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