considered one of the largest families among reader domains. The PHD finger
is made up of 50–80 amino acid residues including a conserved Cys4-His-Cys3
(C4HC3) motif that binds two zinc ions, necessary for the structural integrity of the
domain, in the so-called “cross-braced” manner [25].
Fig. 2 Different families of methyl-binding proteins and their histone targets
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is made up of 50–80 amino acid residues including a conserved Cys4-His-Cys3
(C4HC3) motif that binds two zinc ions, necessary for the structural integrity of the
domain, in the so-called “cross-braced” manner [25].
Fig. 2 Different families of methyl-binding proteins and their histone targets
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