Published June 17, 2016 | Version 5

Human Lysine Demethylase JMJD2D (KDM4D); A Target Enabling Package

Description

There are 4 members of the Lysine Demethylase JMJD2 (KDM4) family. SGC Oxford has expressed, purified and crystallized the catalytic domains of JMJD2A, JMJD2B, JMJD2C and JMJD2D as part of the probe programme. Fragment screening and X-ray crystallography identified a large number of binders, some of which were progressed into a medicinal chemistry programme. Despite significant effort molecules with probe properties were not obtained. Consequently it has been decided to put the information generated into the public domain.

Notes

This document represents version 5 of the TEP datasheet and includes all updates on the project as of October 2018. For more information about TEPs and the TEP Programme, please visit https://thesgc.org/tep.

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Funding

European Commission
ULTRA-DD - Unrestricted Leveraging of Targets for Research Advancement and Drug Discovery 115766