Function
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.
Disease
Relevance
Structural highlights
3D structures of jumonji domain-containing protein 2A
Updated on 01-September-2014
Jmjd2a
2gf7, 2qqr – hJmjd2a double TUDOR domain – human
2gp3 – hJmjd2a catalytic domain + Fe
Jmjd2a binary complex with peptide
2gfa – hJmjd2a double TUDOR domain + peptide with trimethyllysine
2qqs – hJmjd2a double TUDOR domain + histone H4 peptide with trimethyllysine
2oq6, 2os2 – hJmjd2a catalytic domain + Ni + histone H3 peptide with trimethyllysine
2ot7 – hJmjd2a catalytic domain + Ni + histone H3 peptide with methyllysine
2pxj – hJmjd2a catalytic domain + Fe + histone H3 peptide with methyllysine
2ox0 – hJmjd2a catalytic domain + Ni + histone H3 peptide with dimethyllysine
Jmjd2a binary complex with other molecules
2oq7 – hJmjd2a catalytic domain + Ni + oxalylglycine
2vd7, 2wwj, 3njy, 3pdq, 3rvh, 4gd4, 4ai9, 4bis – hJmjd2a catalytic domain + Ni + inhibitor
2gp5 – hJmjd2a catalytic domain + Fe + α-ketoglutarate
2ybk – hJmjd2a catalytic domain + Ni + α-ketoglutarate derivative
Jmjd2a ternary complex
2q8c, 2ybp, 2ybs – hJmjd2a catalytic domain + Fe + histone H3 peptide with trimethyllysine + α-ketoglutarate derivative
2q8d – hJmjd2a catalytic domain + Fe + histone H3 peptide with trimethyllysine + succinate
2q8c, 2p5b – hJmjd2a catalytic domain + Fe + histone H3 peptide with trimethyllysine + oxalylglycine
2q8c – hJmjd2a catalytic domain + Ni + histone H3 peptide with trimethyllysine + oxalylcysteine
References
