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

Pub. Date : 2016 Mar 18

PMID : 26317848






1 Functional Relationships(s)
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1 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. N(2)-methyl-L-lysine L3MBTL histone methyl-lysine binding protein 3 Homo sapiens