The Chodera lab has teamed up with Luo lab at MSKCC to study another important class of cancer targets: protein methyltransferases.
These are protein-modifying enzymes that catalyze the transfer of methyl groups to lysine or arginine residues as part of complex regulatory programs. While a number of cancers have alterations in protein methyltransferases, making them appealing targets for new anticancer therapeutics, it is not yet possible to fully understand their role in disease because of the current limited repertoire of compounds available to selectively inhibit these enzymes.
Spurred by recent encouraging results from the Luo lab in developing sinefungin scaffolds to selectively target key methyltransferases, we are working with them to better understand the origin of selectivity of these compounds, and to help them design new compounds that will allow researchers to better understand the roles these enzymes play in cancer and, eventually, develop potent new anticancer therapeutics.
Projects 10474, 10475, and 10476 study key protein methyltransferases NSD1, NSD2, and SETD2.
