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The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design

Nature Structural Biology volume 3, pages 912915 (1996) | Download Citation

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The crystal structure of Plasmodium falciparum lactate dehydrogenase reveals a surprising shift in the position of the NADH cofactor that explains the unusual biochemical properties of this enzyme. There is also a distinctive surface cleft adjacent to the NADH binding pocket that forms an attractive target for inhibitor design.

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Author information

Affiliations

  1. Molecular Recognition Centre and Department of Biochemistry, University of Bristol School of Medical Sciences, Bristol BS8 1TD UK

    • Cameron R. Dunn
    • , Mark J. Banfield
    • , John J. Barker
    • , Christopher W. Higham
    • , Kathleen M. Moreton
    • , Dilek Turgut-Balik
    • , R. Leo Brady
    •  & J. John Holbrook
  2. l.brady@bris.ac.uk

    • R. Leo Brady

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DOI

https://doi.org/10.1038/nsb1196-912

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