Emily Scott

Dr. Scott’s research focuses on defining relationships between the structures and functional capacities of cytochrome P450 enzymes involved in human drug metabolism or which are drug targets. Her laboratory is best known for structures of human membrane P450 enzymes metabolizing xenobiotics (CYP1A1, CYP2A6, CYP2A13, CYP2E1) and sterols (CYP17A1, CYP11B1, CYP11B2, CYP8B1, CYP3A7), most of which were the first available. Study of xenobiotic-metabolizing P450 enzymes illuminate how drugs and procarcinogens are oxidized by individual P450 enzymes in regio- and stereospecific ways. For P450 enzymes in endogenous biological pathways, Scott lab structures provide guides to the development of inhibitors in disease pathways including prostate cancer, type 2 diabetes, and non-alcoholic fatty liver disease. Additional areas of contribution include P450/protein interactions and dynamics employing solution NMR. Overall, this work enables an understanding of human metabolism to guide the usage of drugs already developed and the design of new pharmaceutical agents.