Joel Harp
Last active: 7/24/2015

The active site of the SET domain is constructed on a knot.

Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S
Nat Struct Biol. 2002 9 (11): 833-8

PMID: 12389038 · DOI:10.1038/nsb861

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.

MeSH Terms (18)

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

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