Journal
FEBS LETTERS
Volume 590, Issue 16, Pages 2776-2786Publisher
WILEY-BLACKWELL
DOI: 10.1002/1873-3468.12276
Keywords
Chagas disease; drug discovery; ternary complex
Funding
- FAPESP (Fundacao de Amparo a Pesquisa do Estado de Sao Paulo) [2013/03983-5]
- BEPE Fellowship [2014/07533-7]
- Wellcome Trust [094090]
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The enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi (TcG6PDH) catalyses the first step of the pentose phosphate pathway (PPP) and is considered a promising target for the discovery of a new drug against Chagas diseases. In the present work, we describe the crystal structure of TcG6PDH obtained in a ternary complex with the substrate -d-glucose-6-phosphate (G6P) and the reduced catalytic' cofactor NADPH, which reveals the molecular basis of substrate and cofactor recognition. A comparison with the homologous human protein sheds light on differences in the cofactor-binding site that might be explored towards the design of new NADP(+) competitive inhibitors targeting the parasite enzyme.
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