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., ...Daha Fazla

NATURE STRUCTURAL BIOLOGY, cilt.3, sa.11, ss.912-915, 1996 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Kısa Makale
  • Cilt numarası: 3 Sayı: 11
  • Basım Tarihi: 1996
  • Doi Numarası: 10.1038/nsb1196-912
  • Dergi Adı: NATURE STRUCTURAL BIOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.912-915
  • Yıldız Teknik Üniversitesi Adresli: Hayır

Özet

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.