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Cell Mol Life Sci. 2006 Dec;63(23):2755-63.

SET domain protein lysine methyltransferases: Structure, specificity and catalysis.

Author information

1
Department of Molecular Physiology and Biophysics, Mount Sinai School of Medicine, New York University, One Gustave L Levy Place, New York, NY 10029, USA.

Abstract

Site- and state-specific lysine methylation of histones is catalyzed by a family of proteins that contain the evolutionarily conserved SET domain and plays a fundamental role in epigenetic regulation of gene activation and silencing in all eukaryotes. The recently determined three-dimensional structures of the SET domains from chromosomal proteins reveal that the core SET domain structure contains a two-domain architecture, consisting of a conserved anti-parallel beta-barrel and a structurally variable insert that surround a unusual knot-like structure that comprises the enzyme active site. These structures of the SET domains, either in the free state or when bound to cofactor S-adenosyl-L-homocysteine and/or histone peptide, mimicking an enzyme/cofactor/substrate complex, further yield the structural insights into the molecular basis of the substrate specificity, methylation multiplicity and the catalytic mechanism of histone lysine methylation.

PMID:
17013555
DOI:
10.1007/s00018-006-6274-5
[Indexed for MEDLINE]

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