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The Structure-Activity Relationships of L3MBTL3 Inhibitors: Flexibility of the Dimer Interface

The Structure-Activity Relationships of L3MBTL3 Inhibitors: Flexibility of the Dimer Interface

Michelle A Camerino, Nan Zhong, Aiping Dong, Bradley M Dickson, Lindsey I James, Brandi M Baughman, Jacqueline L Norris, Dmitri B Kireev, William P Janzen, Cheryl H Arrowsmith, Stephen V Frye

Medchemcomm. 2013 Nov;4(11):1501-1507.

PMID: 24466405

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1415800439	UNC1215		1415800-43-9	Price

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