In this issue of Molecular Cell, Zhang et al. report the structure of a ternary complex between the SET domain histone methyltransferase DIM-5, its cofactor, and a histone H3 peptide. The insight gained from analysis of a key amino acid provides an exciting opportunity to dissect the possible functional meaning of mono-, di-, and trimethylation of histone lysine residues in vivo that will complement existing approaches in the quest to crack the histone methylation code.
In this issue of Molecular Cell , Zhang et al . report the structure of a ternary complex between the SET domain histone methyltransferase DIM-5 , its cofactor , and a histone H3 peptide . The insight gained from analysis of a key amino acid provides an exciting opportunity to dissect the possible functional meaning of mono- , di- , and trimethylation of histone lysine residues in vivo that will complement existing approaches in the quest to crack the histone methylation code .
What is the characteristic domain of histone methyltransferases?
What is the characteristic domain of histone methyltransferases ?
SET domain
SET domain