Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain

Lindsey I. James,Dalia Barsyte-Lovejoy,Nan Zhong,Liubov Krichevsky,Victoria K. Korboukh,J. Martin Herold,Christopher J. MacNevin,Jacqueline L. Norris,Cari A. Sagum,Wolfram Tempel,Edyta Marcon,Hongbo Guo,Cen Gao,Xi Ping Huang,Shili Duan,Andrew Emili,Jack Greenblatt,Dmitri Kireev,Jian Jin,William P. Janzen,Peter J. Brown,Mark T. Bedford,C.H. Arrowsmith,Stephen V. Frye

Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain

2013

Methylation of lysine residues regulates chromatin function in part by recruiting readers to these marks. UNC1215, a selective antagonist of the methyllysine reader L3MBTL3 with a polyvalent mode of interaction, reveals BCLAF1 as a methyllysine-dependent interaction partner for L3MBTL3.

Keywords:

Tumor suppressor proteins
Methyllysine
Methylation
Biochemistry
Posttranslational modification
Drug discovery
Chromatin
Chemical probe
Structural biology
Biology
Molecular probe
Fusion protein
Repressor
DNA-binding protein
Structure–activity relationship

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