One Step Closer To Unlocking Mysteries Of Cancer Drug Development
Chemistry professor Carla Mattos spends much of her time studying a protein known as RAS. It is important in cell proliferation, and until recently has been completely elusive as a drug target, she told News@Northeastern’s Angela Herring.
Once bound to a molecule called guanosine triphosphate, or GTP, RAS can interact with other proteins called effector proteins. Herring writes, “This sets off a cascade of other molecular interactions that allows the cell to reproduce itself. This cellular proliferation doesn’t stop until RAS promotes the hydrolysis of GTP to GDP (guanosine diphosphate).”
Scientists used to think the only way to stop this proliferation was to bind RAS with another protein known as GAP. But two years ago, Mattos’ lab discovered a new mechanism for turning off RAS that is mediated by something called an “allosteric,” or remote, binding site on the protein. When something binds there, RAS’ structure changes, including the part that normally interacts with GAP.
Read Herring’s full article, here.
EDITOR’S NOTE: Angela Herring posted a follow up to her original article on InSolution, Northeastern’s research blog. In this follow up she talks about how Carla Mattos got into studying RAS. You can read that article, here.