Structures of SET domain proteins: protein lysine ...[Cell. 2002]

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1: Cell. 2002 Oct 4;111(1):5-7. Links

Structures of SET domain proteins: protein lysine methyltransferases make their mark.

Yeates TO.

UCLA Molecular Biology Institute and Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, 611 Charles Young Dr. East, Box 951570, Los Angeles, CA 90095, USA. yeates@mbi.ucla.edu

Proteins bearing the widely distributed SET domain have been shown to methylate lysine residues in histones and other proteins. In this issue, three-dimensional structures are reported for three very different SET domain-containing proteins. The structures reveal novel folds for several new domains, including SET, and provide early insights into mechanisms of catalysis and molecular recognition in this family of enzymes.

PMID: 12372294 [PubMed - indexed for MEDLINE]

Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. [Cell. 2002]
Crystal structure and functional analysis of the histone methyltransferase SET7/9. [Cell. 2002]
Structure and catalytic mechanism of a SET domain protein methyltransferase. [Cell. 2002]
SET domain protein lysine methyltransferases: Structure, specificity and catalysis. [Cell Mol Life Sci. 2006]
Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. [Biochem Biophys Res Commun. 2006]
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Structures of SET domain proteins: protein lysine methyltransferases make their mark.

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