This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Histone deacetylase
From Proteopedia
| Line 4: | Line 4: | ||
* [[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]]. | ||
| - | |||
| - | {{TOC limit|limit=2}} | ||
== 3D Structures of histone deacetylase == | == 3D Structures of histone deacetylase == | ||
Revision as of 10:44, 18 August 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 18-August-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
