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Structure of a novel dimeric SET domain methyltransferase that regulates cell motility
Lysine methyltransferases (KMTs) were initially associated with transcriptional control through their methylation of histones and other nuclear proteins, but have since been found to regulate many other cellular activities. The apical complex lysine (K) methyltransferase (AKMT) of the human parasite Toxoplasma gondii was recently shown to play a critical role in regulating cellular motility. Here we report a 2.1-Å resolution crystal structure of the conserved and functional C-terminal portiondoi:10.1101/264291 fatcat:cynmltdhuzdjpb65hqrdny2pla