Description
There are 3 members of the Lysine Demethylase JMJD1 (KDM3) family, JMJD1A-C. SGC Oxford has expressed, purified and crystallized the catalytic domains of JMJD1A, JMJD1B and JMJD1C 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.
Resources
| Name | Format | Description | Link |
|---|---|---|---|
| Unknown Resource | Unknown | Open resource | |
| Unknown Resource | Unknown | Open resource |
Tags
- cancer
- chemical-biology
- chemical-probe
- disease
- drug-discovery
- drug-target
- genetics
- infectious-disease
- jmjd1b
- kdm3b
- malaria
- metabolic-diseases
- neuro
- neurological-genetic-disorders
- neuropsychiatry
- oncology
- orphan-disease
- protein
- structural-genomics
- structure
- structure-discovery
- target-enabling-package