This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Protein arginine methyltransferases (PRMTs) have been implicated in many biological processes, such as post-translation, transcription, and DNA repair. Loss of the arginine methylation at specific-sites have been documented in various tumors of the breast, lung, pancreas, and prostate. PRMTs are classified either as type I, type II or type III based on the nature of the methylation of the nitrogen atom at the arginine side-chain. Both type I and II enzymes transfer one methyl group from S-adenosylmethionine (+AdoMet) to N?-monomethylation. Type I enzyme can catalyzes N?-N?-asymmetric di-methylation, while type II catalyzes N?-N?-symmetric di-methylation. Type III enzymes generate N? mono-methylation. The first step in arginine methylation is deprotonation to form the arginine base nucleophile. How the different type of PRMTs chooses the different deprotonation state of arginine is a crucial question for understanding of the mechanism by special PRMT. The potential of mean force will be carried out in the solvent to investigate the mechanism of methylation.
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