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Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii). Chemical communications (Cambridge, England) [Chem Commun (Camb)] Journal article

 
Sekirnik R, Rose NR, Thalhammer A, Seden PT, Mecinović J, Schofield CJ 
Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii). [Journal Article]
Chem Commun (Camb) 2009 Nov 14; (42):6376-8.


JMJD2A, a 2-oxoglutarate dependent N(epsilon)-methyl lysine histone demethylase, is inhibited by disruption of its Zn-binding site by Zn-ejecting compounds including disulfiram and ebselen; this observation may enable the development of inhibitors selective for this subfamily of 2OG dependent oxygenases that do not rely on binding to the highly-conserved Fe(ii)-containing active site.



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