Structural and histone binding studies of the chromo barrel domain of TIP 60

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Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4.

We have determined the human male specific lethal 3 (hMSL3) chromo-barrel domain structure by x-ray crystallography to a resolution of 2.5 Å (r = 0.226, R(free) = 0.270). hMSL3 contains a canonical methyllysine binding pocket made up of residues Tyr-31, Phe-56, Trp-59, and Trp-63. A six-residue insertion between strands β(1) and β(2) of the hMSL3 chromo-barrel domain directs the side chain of G...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 2018

ISSN: 0014-5793,1873-3468

DOI: 10.1002/1873-3468.13021