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Issue 11, 2013
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The structure–activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface

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Abstract

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.

Graphical abstract: The structure–activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface

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Publication details

The article was received on 11 Jul 2013, accepted on 16 Sep 2013 and first published on 17 Sep 2013


Article type: Concise Article
DOI: 10.1039/C3MD00197K
Citation: Med. Chem. Commun., 2013,4, 1501-1507
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    The structure–activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface

    M. A. Camerino, N. Zhong, A. Dong, B. M. Dickson, L. I. James, B. M. Baughman, J. L. Norris, D. B. Kireev, W. P. Janzen, C. H. Arrowsmith and S. V. Frye, Med. Chem. Commun., 2013, 4, 1501
    DOI: 10.1039/C3MD00197K

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