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The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.

Original publication




Journal article


Nature structural biology

Publication Date





833 - 838


Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, Virginia 22908, USA.


Humans, Coenzymes, Methyltransferases, Protein Methyltransferases, Histone-Lysine N-Methyltransferase, S-Adenosylhomocysteine, Recombinant Proteins, Crystallography, X-Ray, Magnetic Resonance Spectroscopy, Sequence Alignment, Binding Sites, Amino Acid Sequence, Conserved Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Models, Molecular, Molecular Sequence Data, Histone Methyltransferases