| Texto completo | |
| Autor(es): |
Mercaldi, Gustavo F.
;
Dawson, Alice
;
Hunter, Willian N.
;
Cordeiro, Artur T.
Número total de Autores: 4
|
| Tipo de documento: | Artigo Científico |
| Fonte: | FEBS Letters; v. 590, n. 16, p. 11-pg., 2016-08-01. |
| Resumo | |
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. (AU) | |
| Processo FAPESP: | 13/03983-5 - Estudos funcionais e estruturais das enzimas relacionadas a produção de NADPH em trypanosomatídeos |
| Beneficiário: | Artur Torres Cordeiro |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 14/07533-7 - Estudos biofísicos de complexos da glicose 6-fosfato desidrogenase com inibidores |
| Beneficiário: | Gustavo Fernando Mercaldi |
| Modalidade de apoio: | Bolsas no Exterior - Estágio de Pesquisa - Doutorado |