Jumonji domain-containing protein

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== Function ==
== Function ==
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'''Jumonji domain-containing protein 2A''' (Jmjd2a) catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36 producing the dimethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains (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.
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'''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.
== Disease ==
== Disease ==

Revision as of 08:36, 4 April 2016

Structure of human Jumonji domain-containing protein 2A catalytic domain complex with oxalylglycine, Fe+2 ion, Zn+2 ion (grey) and histone H3 peptide with trimethyllysine (aqua and wheat) (PDB code 2p5b).

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3D structures of jumonji domain-containing protein 2A

Updated on 04-April-2016


References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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