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Structural basis of kynurenine 3-monooxygenase inhibition

Author

Listed:
  • Marta Amaral

    (Manchester Institute of Biotechnology, The University of Manchester
    University of Leicester
    Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular
    Instituto de Fisiologia)

  • 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
    Instituto de Fisiologia
    Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center Göttingen, Waldweg 33, 37073 Göttingen, Germany)

  • 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)

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.

Suggested Citation

  • Marta Amaral & Colin Levy & Derren J. Heyes & Pierre Lafite & Tiago F. Outeiro & Flaviano Giorgini & David Leys & Nigel S. Scrutton, 2013. "Structural basis of kynurenine 3-monooxygenase inhibition," Nature, Nature, vol. 496(7445), pages 382-385, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7445:d:10.1038_nature12039
    DOI: 10.1038/nature12039
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