Angela Smith (University of Notre Dame)

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Location: 244 DeBartolo Hall

Abstract:   KRAS is one of the most frequently mutated proteins in cancers and has been considered undruggable for the past few decades. The recent discovery of covalent inhibitors targeting the KRAS-G12C mutation has show that it is possible to inhibit KRAS with high potency in vitroand in vivo. Through an extensive investigation of the biochemical mechanism of these inhibitors, this paper highlights how a target lacking conventional binding pockets can still be inhibited with high potency.

Citation:   Hansen, R., Peters, U., Babbar, A., Chen, Y., Feng, J., Janes, M.R., Li, L., Ren, P., Liu, Y., Zarrinkar, P.P. The reactivity-driven biochemical mechanism of covalent KRASG12Cinhibitors. Nat. Struct. Mol. Biol.25, 454-462 (2018).

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