The active site of the SET domain is constructed on a knot
- 21 October 2002
- journal article
- letter
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 9 (11) , 833-8
- https://doi.org/10.1038/nsb861
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.Keywords
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