News and Views


Nature Structural & Molecular Biology 14, 682 - 684 (2007)
doi:10.1038/nsmb0807-682

Targeting the JMJD2A histone lysine demethylase

Jon R Wilson1

  1. Jon Wilson is in the Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK. e-mail: jon.wilson@icr.ac.uk


Targeting of enzymes regulating chromatin organization to specific histone residues is a key element in the hugely complex system of epigenetic signaling that controls gene regulation and repair. Understanding of how targeting is achieved is still limited, but structures of the histone lysine demethylase JMJD2A in complex with substrate peptides now offer insight into its dual specificity.

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