Interaction of human dihydroorotate dehydrogenase with ubiquinone in model lipid bilayers
Human dihydroorotate dehydrogenase (DHODH) is an integral membrane protein involved in pyrimidine biosynthesis. DHODH is a well-validated target for anti-inflammatory and anti-proliferative drugs that act as inhibitors. Mutations in DHODH cause Miller syndrome, a rare genetic disorder. DHODH contains two amphipathic alpha helices proposed to be critical for its interaction with the membrane, with its co-substrate ubiquinone Q10 and with inhibitors. Our goal is to investigate the mechanisms by which these interactions occur in a physiologically relevant membrane-bound state consisting of oriented planar lipid bilayers using neutron reflectivity. We have previously performed a successful experiment to investigate the formation and structure of lipid bilayers containing ubiquinone Q10 and a shorter derivative (ubiquinone Q2). As a continuation, we propose to investigate the interaction of N-terminally truncated DHODH (consisting of the catalytic domain and membrane-binding helices) with lipid bilayers containing either ubiquinone Q2 or Q10.
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OROZCO RODRIGUEZ Juan Manuel; BOGOJEVIC Oliver; DELHOM Robin; FRAGNETO Giovanna; KNECHT Wolfgang and WACKLIN KNECHT Hanna. (2019). Interaction of human dihydroorotate dehydrogenase with ubiquinone in model lipid bilayers. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-821
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