Structural basis of kynurenine 3-monooxygenase inhibition

Marta Amaral, Colin Levy, Derren J. Heyes, Pierre Lafite, Tiago F. Outeiro, Flaviano Giorgini, David Leys and Nigel S. Scrutton ()
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Marta Amaral: Manchester Institute of Biotechnology, The University of Manchester
Colin Levy: Manchester Institute of Biotechnology, The University of Manchester
Derren J. Heyes: Manchester Institute of Biotechnology, The University of Manchester
Pierre Lafite: Institut de Chimie Organique et Analytique, Université d’Orléans, CNRS UMR 7311 BP6769, Rue de Chartres, 45067 Orléans Cedex 2, France
Tiago F. Outeiro: Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular
Flaviano Giorgini: University of Leicester
David Leys: Manchester Institute of Biotechnology, The University of Manchester
Nigel S. Scrutton: Manchester Institute of Biotechnology, The University of Manchester

Nature, 2013, vol. 496, issue 7445, 382-385

Abstract: Inhibition of kynurenine 3-monooxygenase (KMO) leads to amelioration of Huntington’s-disease-relevant phenotypes in yeast, fruitfly and mouse models; here the crystal structures of free and inhibitor-bound yeast KMO are presented, which could aid the development of targeted therapies for human neurodegenerative diseases.

Date: 2013
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DOI: 10.1038/nature12039

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