Jumonji domain-containing protein: Difference between revisions
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<StructureSection load='2p5b' size='450' side='right' caption='Structure of human Jumonji domain-containing protein 2a catalytic domain complex with oxalylglycine, Fe+2 ion, Zn+2 ion (grey) and histone H3 peptide (aqua) with trimethyllysine (magenta) (PDB code [[2p5b]]).' scene='59/596434/Cv/1'> | <StructureSection load='2p5b' size='450' side='right' caption='Structure of human Jumonji domain-containing protein 2a catalytic domain complex with oxalylglycine, Fe+2 ion, Zn+2 ion (grey) and histone H3 peptide (aqua) with trimethyllysine (magenta) (PDB code [[2p5b]]).' scene='59/596434/Cv/1'> | ||
SEE ALSO [[Lysine-specific histone demethylase]] | |||
== Function == | == Function == | ||
*'''Jumonji domain-containing protein 2a''' (Jmjd2a) or '''KDM4A''' catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 producing the dimethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains which recognize dimethylated Arg (residues 895-1011) , 2 PHD-type zinc fingers and C-terminal domain. Jmjd2a is Fe+2 and α-ketoglutarate dependent. Methylation of histones in the chromatin is involved in regulation of gene activity, chromatin structure and epigenetic memory<ref>PMID:16677698</ref>.<br /> | *'''Jumonji domain-containing protein 2a''' (Jmjd2a) or '''KDM4A''' catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 producing the dimethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains which recognize dimethylated Arg (residues 895-1011) , 2 PHD-type zinc fingers and C-terminal domain. Jmjd2a is Fe+2 and α-ketoglutarate dependent. Methylation of histones in the chromatin is involved in regulation of gene activity, chromatin structure and epigenetic memory<ref>PMID:16677698</ref>.<br /> | ||