title: Structures of SET domain proteins: protein lysine methyltransferases make their mark.
abstract: 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.
authors.affiliation: 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
authors.forename: Todd O
authors.initials: TO
authors.lastname: Yeates
mesh_terms: D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry*; D029721:Drosophila Proteins / Q000737:chemistry*; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry*; D006657:Histones / Q000737:chemistry; D008780:Methyltransferases / Q000737:chemistry; D008958:Models, Molecular; D009491:Neurospora / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry*; D063151:Polycomb Repressive Complex 2; D011487:Protein Conformation; D011496:Protein Methyltransferases; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry*; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry; D014157:Transcription Factors
chemical_list: D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D006657:Histones; D009687:Nuclear Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; C063460:Trl protein, Drosophila; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; C083329:E(z) protein, Drosophila; D011495:Histone-Lysine N-Methyltransferase; D063151:Polycomb Repressive Complex 2; D012273:Ribulose-Bisphosphate Carboxylase