BioTech Mag Search: Energy
Engineering Human JMJD2A Tudor Domains For An Improved Understanding of Histone Peptide Recognition
13 days ago - By Wiley
Abstract
JMJD2A is a histone lysine demethylase which recognizes and demethylates H3K9me3 and H3K36me3 residues and is overexpressed in various cancers. It utilizes a tandem tudor domain to facilitate its own recruitment to histone sites, recognizing various di- and tri-methyl lysine residues with moderate affinity. In this study, we successfully engineered the tudor domain of JMJD2A to specifically bind to H4K20me3 with a 20-fold increase of affinity and improved selectivity. To reveal the molecular basis, we performed molecular dynamics and free energy decomposition analysis on the human...
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2nd International Conference on Generic Drugs and Biosimilars
2nd International Conference on Generic Drugs and Biosimilars
2nd International Conference on Generic Drugs and Biosimilars
2nd International Conference on Generic Drugs and Biosimilars
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