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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.

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