pArg50Gly

pArg50Gly is a post-translational modification that occurs on proteins, specifically on the arginine residue at position 50. This modification involves the addition of a glycine residue to the arginine side chain, forming a peptide bond between the arginine and glycine. The process is catalyzed by the enzyme peptidylarginine deiminase 4 (PAD4), which converts the arginine to citrulline and then adds the glycine.

pArg50Gly is found in various proteins and is involved in several biological processes. It is often associated with the regulation of protein-protein interactions, as the addition of the glycine residue can alter the protein's structure and function. This modification has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. For example, pArg50Gly has been shown to regulate the activity of certain transcription factors, which are key regulators of gene expression.

The identification and characterization of pArg50Gly have advanced our understanding of protein regulation and its role in disease. However, the precise mechanisms by which pArg50Gly contributes to disease pathogenesis and potential therapeutic targets remain areas of active research.