Nature Structural Biology
3, 912 - 915 (1996)
doi:10.1038/nsb1196-912
The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial designCameron R. Dunn1, Mark J. Banfield1, John J. Barker1, Christopher W. Higham1, Kathleen M. Moreton1, Dilek Turgut-Balik1, R. Leo Brady1, 2
& J. John Holbrook1
1Molecular Recognition Centre and Department of Biochemistry, University of Bristol School of Medical Sciences, Bristol BS8 1TD UK
2l.brady@bris.ac.uk 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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