Structural origins for the product specificity of SET domain protein methyltransferases

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 105; no. 52; pp. 20659 - 20664
• Main Authors: Couture, Jean-François, Dirk, Lynnette M.A, Brunzelle, Joseph S, Houtz, Robert L, Trievel, Raymond C
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 30.12.2008; National Acad Sciences
• Subjects: 08 HYDROGEN; Active sites; AFFINITY; Amino Acid Substitution; Ammonium; BEARINGS; Biochemical mechanisms; Biochemistry; Biological Sciences; BONDING; Catalysis; Catalytic Domain - genetics; CHAINS; Chemical reactions; CRYSTAL STRUCTURE; Crystallography, X-Ray; DISSOCIATION; Enzymes; Histone-Lysine N-Methyltransferase - chemistry; Histone-Lysine N-Methyltransferase - genetics; HISTONES; Humans; HYDROGEN; hydrogen bonding; Hydrogen bonds; LYSINE; METHYLATION; methyltransferases; Molecules; MUTANTS; Mutation, Missense; PEPTIDES; PHENYLALANINE; Protein Structure, Tertiary - genetics; PROTEINS; Reaction kinetics; Solvents; SPECIFICITY; Substrate Specificity - genetics; SUBSTRATES; TRANSCRIPTION; WATER; Water conservation

SET domain protein lysine methyltransferases (PKMTs) regulate transcription and other cellular functions through site-specific methylation of histones and other substrates. PKMTs catalyze the formation of monomethylated, dimethylated, or trimethylated products, establishing an additional hierarchy w...