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 In both proteins, the walls of the lysine-binding channel are shaped by hydrophobic residues that engage in van der Waals interactions with the lysine side chain (Determine 4b,c ). On the base of the channel is the methyltransfer pore, which connects the pocket to the AdoMet-binding cleft. Min J, Zhang X, Cheng X, Grewal SI, Xu RM: Structure of the SET domain histone lysine methyltransferase Clr4.
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