Histone deacetylase

spinqualitylabelsall models Human sirtuin-3 complex with peptide containing acetylated lysine, sulfate, carbonate, glycerol and Zn+2 ion (PDB entry 3glr) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function 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. SAHA is a common inhibitor of HDAC. HDAC are classified according to their domain organization into 4 classes. HDAC class I are homologous to yeast Rpd3. HDAC class II are homologous to yeast HdaI. HDAC class IIa lack enzymatic activity. HDAC class III called sirtuin - (Silent Information Regulator) (SIRT) are NAD-dependent HDAC. This protein is bifunctional and can act as a deacylase or as mono-ADP-acetyltransferase. . HDAC Rpd3 belongs to class I and is involved in transcriptional repression . HDAC Clr (Cryptic Loci Regulator) is responsible of deacetylation of Lys residues at the N-terminal of histones . For HDAC8 see - Histone deacetylase 8 (HDAC8). For additional details see Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure Transcription and RNA Processing. Relevance HDAC inhibitors are used in cancer therapy. Sirtuins play a role in cancer, metabolic activity and neurodegenerative diseases. HDAC inhibitor SAHA or Zolinza (Vorinostat) is used in the treatment of cutaneous T cell lymphoma. Structural highlights The biological assembly of Human sirtuin-3 is homodimer. The acetylated lysine of the peptide is inserted in an extended conformation between the 2 domains of SIRT3 - a large Rossman fold, NAD-binding domain and a small Zn-binding one). Water molecule shown as red sphere. 3D Structures of histone deacetylase Histone deacetylase 3D structures

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