Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii)
- 28 September 2009
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- No. 42,p. 6376-6378
- https://doi.org/10.1039/b916357c
Abstract
JMJD2A, a 2-oxoglutarate dependent Nε-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.Keywords
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