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Structure of histone H3 K4-specific methyltransferase SET7/9Structure of histone H3 K4-specific methyltransferase SET7/9
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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 Nov;9(11):833-8. PMID:12389038[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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