Literature summary for 1.14.11.66 extracted from

Ng, S.S.; Kavanagh, K.L.; McDonough, M.A.; Butler, D.; Pilka, E.S.; Lienard, B.M.; Bray, J.E.; Savitsky, P.; Gileadi, O.; von Delft, F.; Rose, N.R.; Offer, J.; Scheinost, J.C.; Borowski, T.; Sundstrom, M.; Schofield, C.J.; Oppermann, U.
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity (2007), Nature, 448, 87-91.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of JMJD2A-Ni(II)-Zn(II) inhibitor complexes bound to tri-, di- and monomethyl forms of histone 3 lysine 9 and the trimethyl form of histone 3 lysine 36. The structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn-binding site. The mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate	Homo sapiens

Crystallization (Comment)

Organism

structures of JMJD2A-Ni(II)-Zn(II) inhibitor complexes bound to tri-, di- and monomethyl forms of histone 3 lysine 9 and the trimethyl form of histone 3 lysine 36. The structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn-binding site. The mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	the mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O75164	isoform JMJD2A	-

Synonyms

Synonyms	Comment	Organism
JMJD2A	-	Homo sapiens

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Release 2023.1 (January 2023)