Histone methyltransferase: Difference between revisions
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<StructureSection load='1o9s' size='350' side='right' caption='Human histone-lysine N-methyltrasferase | <StructureSection load='1o9s' size='350' side='right' caption='Human histone-lysine N-methyltrasferase (grey, green) complex with methylated lysine histone H3 peptide (rust, aqua) and S-adenosyl homocysteine (SAH) (PDB entry [[1o9s]])' scene=''> | ||
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
Inhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy | Inhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy drug<ref>PMID:21782458</ref>.s. | ||
== Disease == | == Disease == | ||
Aberrant HMT plays a role in cancer, intellectual disability syndromes and regulation of tissue aging<ref>PMID:22473383</ref>. | Aberrant HMT plays a role in cancer, intellectual disability syndromes and regulation of tissue aging<ref>PMID:22473383</ref>. | ||
== 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<ref>PMID:12540855</ref>. | |||
</StructureSection> | |||
== 3D Structures of histone methyltransferase == | == 3D Structures of histone methyltransferase == | ||