Download MendeleyA potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana.
Suresh, S., Turley, S., Opperdoes, F.R., Michels, P.A., Hol, W.G.(2000) Structure 8: 541-552
- PubMed: 10801498
- DOI: https://doi.org/10.1016/s0969-2126(00)00135-0
- Primary Citation of Related Structures:
1EVY, 1EVZ - PubMed Abstract:
NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. Although the enzyme has been characterized and cloned from a number of sources, until now no three-dimensional structure has been determined for this enzyme. Although the utility of this enzyme as a drug target against Leishmania mexicana is yet to be established, the critical role played by GPDH in the long slender bloodstream form of the related kinetoplastid Trypanosoma brucei makes it a viable drug target against sleeping sickness.
Organizational Affiliation:
Department of Biological Structure, Biomolecular Structure Center, Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
