Histone methyltransferase

spinqualitylabelsall models Human histone-lysine N-methyltrasferase (magenta) complex with methylated lysine histone H3 peptide (green) and S-adenosyl homocysteine (SAH) (PDB entry 1o9s) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Histone methyltransferase (HMT) are histone-lysine N-methyltransferase (KHMT) and histone-arginine N-methyltransferase (RHMT) which catalyzes the transfer of methyl groups to lysine and arginine residues of histones. HMT use S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) as the methyl donor. KHMT can be SET domain-containing or non-SET domain-containing. The SET domain contains the catalytic core of KHMT and targets the lysine tail region of KHMT. CxxC domain is a zinc finger domain. For SET7/9 see Histone Lysine Methyltransferase SET7/9. euchromatin histone methyltransferase dimethylates histone H3 at Lys 9 resulting in transcriptional repression. DOT1L histone methyltransferase methylates histone H3 at Lys 79 resulting in transcriptional repression. Relevance Inhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy drugs. Disease Aberrant HMT plays a role in cancer, intellectual disability syndromes and regulation of tissue aging. Structural highlights Human KHMT binds SAH in the peptide binding groove with the histone H3 peptide assuming an extended conformation and the methylated lysine inserted in a hydrophobic environment. Water molecules shown as red spheres 3D Structures of histone methyltransferase Histone methyltransferase 3D structures

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