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

Dunn C., Banfield M., Barker J., Higham C., Moreton K., Turgut-Balik D., ...More

NATURE STRUCTURAL BIOLOGY, vol.3, no.11, pp.912-915, 1996 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Letter
  • Volume: 3 Issue: 11
  • Publication Date: 1996
  • Doi Number: 10.1038/nsb1196-912
  • Journal Name: NATURE STRUCTURAL BIOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.912-915
  • Yıldız Technical University Affiliated: No

Abstract

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.