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

Article Details

Citation

Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S

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

Nat Struct Biol. 2002 Nov;9(11):833-8.

PubMed ID
12389038 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Histone-lysine N-methyltransferase SETD7Q8WTS6Details