title: Molecular Recognition of Lys and Arg Methylation.
abstract: A network of reader proteins and enzymes precisely controls gene transcription through the dynamic addition, removal, and recognition of post-translational modifications (PTMs) of histone tails. Histone PTMs work in concert with this network to regulate gene transcription through the histone code, and the dysregulation of PTM maintenance is linked to a large number of diseases, including many types of cancer. A wealth of research aims to elucidate the functions of this code, but our understanding of the effects of PTMs, specifically the methylation of lysine (Lys) and arginine (Arg), is lacking. The development of new tools to study PTMs relies on a sophisticated understanding of the mechanisms that drive protein and small molecule recognition in water. In this review, we outline the physical organic concepts that drive the molecular recognition of Lys and Arg methylation by reader proteins and draw comparisons to the binding mechanisms of small molecule receptors for methylated Lys and Arg that have been developed recently.
authors.affiliation: Department of Chemistry, University of North Carolina , CB 3290, Chapel Hill, North Carolina 27599, United States.
authors.forename: Joshua E
authors.initials: JE
authors.lastname: Beaver
authors.affiliation: Department of Chemistry, University of North Carolina , CB 3290, Chapel Hill, North Carolina 27599, United States.
authors.forename: Marcey L
authors.initials: ML
authors.lastname: Waters
mesh_terms: D001120:Arginine / Q000737:chemistry / Q000378:metabolism*; D044127:Epigenesis, Genetic; D006801:Humans; D008239:Lysine / Q000737:chemistry / Q000378:metabolism*; D008745:Methylation; D011485:Protein Binding; D011499:Protein Processing, Post-Translational
chemical_list: D001120:Arginine; D008239:Lysine