Jumonji domain-containing protein: Difference between revisions
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== Function == | == Function == | ||
'''Jumonji domain-containing protein 2A''' (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the demethylated 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. | '''Jumonji domain-containing protein 2A''' (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the demethylated 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>. | ||
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
Jmjd2a uses 9 residues for interaction with the methylated peptide and 4 residues are involved with binding to the peptide's trimethyllysine moiety. An O2 molecule is recruited into the catalytic center<ref>PMID:17567753</ref>. | |||
</StructureSection> | </StructureSection> | ||