Jumonji domain-containing protein: Difference between revisions
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<StructureSection load='2p5b' size=' | <StructureSection load='2p5b' size='350' 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]] | 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''' or '''Lysine-specific demethylase''' 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 2b''' (Jmjd2b) or '''KDM4B''' and '''Jumonji domain-containing protein 2d''' (Jmjd2d) or '''KDM4D''' catalyze the demethylation of trimethylated histone H3 at lysine residues 9 producing the dimethylated form. <br /> | *'''Jumonji domain-containing protein 2b''' (Jmjd2b) or '''KDM4B''' and '''Jumonji domain-containing protein 2d''' (Jmjd2d) or '''KDM4D''' catalyze the demethylation of trimethylated histone H3 at lysine residues 9 producing the dimethylated form. <br /> | ||
*'''Jumonji domain-containing protein 3''' (Jmjd3) or '''KDM6B''' and '''Jumonji domain-containing protein 2d''' (Jmjd2d) or '''KDM4D''' catalyze the demethylation of trimethylated histone H3 at lysine residues 27 producing the dimethylated form<ref>PMID:22308433</ref>. <br /> | *'''Jumonji domain-containing protein 3''' (Jmjd3) or '''KDM6B''' and '''Jumonji domain-containing protein 2d''' (Jmjd2d) or '''KDM4D''' catalyze the demethylation of trimethylated histone H3 at lysine residues 27 producing the dimethylated form<ref>PMID:22308433</ref>. <br /> | ||
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**[[4qxc]] – mJmj1a residues 36-364 + Ni + oxalylglycine + H3 peptide <br /> | **[[4qxc]] – mJmj1a residues 36-364 + Ni + oxalylglycine + H3 peptide <br /> | ||
**[[4qx8]], [[4qx7]], [[4qwn]] – mJmj1a residues 36-364 + Ni + oxoglutarate + H3 peptide <br /> | **[[4qx8]], [[4qx7]], [[4qwn]] – mJmj1a residues 36-364 + Ni + oxoglutarate + H3 peptide <br /> | ||
* Lysine-specific demethylase 5C; KDM5C; JARID1C | |||
**[[5fwj]] – hLSD5C Jmj domain + inhibitor<br /> | |||
**[[2jrz]] – hLSD5C Bright/ARID domain - NMR<br /> | |||
*lysine-specific demethylase 5D or JARID1D | |||
**[[2yqe]] – hLSD5D ARID domain - NMR<br /> | |||
*Jmjd1b (Lysine-specific demethylase 2B; KDM2B) | *Jmjd1b (Lysine-specific demethylase 2B; KDM2B) | ||