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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.
The work at the SGC has been supported by the Innovative Medicines Initiative Joint Undertaking (IMI JU) under grant agreement [115766]. This document represents version 3 of the TEP datasheet and includes all updates on the project as of April 2018. For more information about TEPs and the TEP Programme, please visit https://thesgc.org/tep.
disease, structure discovery, infectious disease, JMJD2D, malaria, chemical probe, chemical biology, structural genomics, metabolic diseases, drug target, drug discovery, neurological genetic disorders, KDM4D, target enabling package, cancer, neuropsychiatry, neuro, genetics, structure, orphan disease, protein
disease, structure discovery, infectious disease, JMJD2D, malaria, chemical probe, chemical biology, structural genomics, metabolic diseases, drug target, drug discovery, neurological genetic disorders, KDM4D, target enabling package, cancer, neuropsychiatry, neuro, genetics, structure, orphan disease, protein
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