Histone deacetylase
From Proteopedia
(Difference between revisions)
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**[[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 /> | ||
+ | **[[4qa1]], [[4qa2]], [[4qa3]], [[4qa4]] - hHDAC8 (mutant) + inhibitor<br /> | ||
+ | **[[2v5w]] – hHDAC8 + tripeptide substrate<br /> | ||
+ | **[[4qa5]], [[4qa6]], [[4qa7]], [[3ewf]] - hHDAC8 (mutant) + tetrapeptide substrate<br /> | ||
+ | **[[3rqd]] - hHDAC8 + largazole<br /> | ||
+ | **[[4rn0]], [[4rn1]], [[4rn2]] - hHDAC8 (mutant) + largazole analog<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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**[[3mz6]] - hHDAC8 (Fe) (mutant) + amide derivative<br /> | **[[3mz6]] - hHDAC8 (Fe) (mutant) + amide derivative<br /> | ||
**[[2v5x]] - hHDAC8 (mutant) + octanediamide derivative<br /> | **[[2v5x]] - hHDAC8 (mutant) + octanediamide derivative<br /> | ||
- | **[[2v5w]] – hHDAC8 + tripeptide<br /> | ||
- | **[[3ewf]] - hHDAC8 (mutant) + polypeptide<br /> | ||
- | **[[3rqd]] - hHDAC8 + largazole<br /> | ||
**[[4bz5]] – SmHDAC8 – ''Schistosoma mansoni''<br /> | **[[4bz5]] – SmHDAC8 – ''Schistosoma mansoni''<br /> | ||
- | **[[4bz7]], [[4bz8]], [[4bz9]] – SmHDAC8 + inhibitor<br /> | + | **[[4bz7]], [[4bz8]], [[4bz9]], [[4cqf]] – SmHDAC8 + inhibitor<br /> |
**[[4bz6]] – SmHDAC8 + SAHA<br /> | **[[4bz6]] – SmHDAC8 + SAHA<br /> | ||
Revision as of 09:04, 21 April 2015
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.
3D Structures of histone deacetylase
Updated on 21-April-2015