1225280-80-7Relevant articles and documents
The structure-activity relationships of L3MBTL3 inhibitors: Flexibility of the dimer interface
Camerino, Michelle A.,Zhong, Nan,Dong, Aiping,Dickson, Bradley M.,James, Lindsey I.,Baughman, Brandi M.,Norris, Jacqueline L.,Kireev, Dmitri B.,Janzen, William P.,Arrowsmith, Cheryl H.,Frye, Stephen V.
supporting information, p. 1501 - 1507 (2013/11/19)
We recently reported the discovery of UNC1215, a potent and selective chemical probe for the L3MBTL3 methyllysine reader domain. In this article, we describe the development of structure-activity relationships (SAR) of a second series of potent L3MBTL3 antagonists which evolved from the structure of the chemical probe UNC1215. These compounds are selective for L3MBTL3 against a panel of methyllysine reader proteins, particularly the related MBT family proteins, L3MBTL1 and MBTD1. A co-crystal structure of L3MBTL3 and one of the most potent compounds suggests that the L3MBTL3 dimer rotates about the dimer interface to accommodate ligand binding.
