Summarized by Plex Health
Last Updated: 10 May 2022

Particular lysine residues on histone tails can be methylated by protein lysine methyltransferases using S-adenosyl-L-methionine as the methyl donor. Since the methylation states of the target lysines play a basic role in the regulation of chromatin structure and gene expression, it is essential to examine the property of PKMTs that enables a specific number of methyl groups to be added. The free energy obstacles of the methyl transfer processes calculated from our simulations follow speculative information, supporting the suggestion that the relative free energy barriers may identify, at least in part, the item specificity of PKMTs. The changes of the free energy obstacles as an outcome of the mutations are additionally talked about based on the structural details gotten from the simulations. The results suggest that the space and active-site interactions around the -amino group of the target lysine readily available for methyl enhancement appear to among the crucial structural factors in controlling the item uniqueness and task of PKMTs.

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