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Article

The L3MBTL3 Methyl-Lysine Reader Domain Functions As a Dimer.

ACS chemical biology - 18 Mar 2016

Baughman Brandi M, Pattenden Samantha G, Norris Jacqueline L, James Lindsey I, Frye Stephen V

Abstract excerpt

L3MBTL3 recognizes mono- and dimethylated lysine residues on histone tails. The recently reported X-ray cocrystal structures of the chemical probe UNC1215 and inhibitor UNC2533 bound to the methyl-lysine reading MBT domains of L3MBTL3 demonstrate a unique and flexible 2:2 dimer mode of recognition. In this study, we describe our in vitro analysis of L3MBTL3 dimerization via its MBT domains and additionally show...

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Identifiers

PMID: 26317848
DOI: 10.1021/acschembio.5b00632
PMCID: PMC4775453

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