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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

DOI

10.1038/nsb861

Type

Journal article

Journal

Nature structural biology

Publication Date

11/2002

Volume

9

Pages

833 - 838

Addresses

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

Keywords

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