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Abstract
The enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi (TcG6PDH) catalyses the first step of the pentose phosphate pathway 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 glucose-6-phosphate 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. This article is protected by copyright. All rights reserved.
Original language | English |
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Pages (from-to) | 2776-2786 |
Number of pages | 11 |
Journal | FEBS Letters |
Volume | 590 |
Issue number | 16 |
Early online date | 19 Jul 2016 |
DOIs | |
Publication status | Published - 19 Aug 2016 |
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Dive into the research topics of 'The structure of a Trypanosoma cruzi glucose-6-phosphate dehydrogenase reveals differences from the mammalian enzyme'. Together they form a unique fingerprint.Projects
- 1 Finished
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State-of-the-Art Facilities for Structural Biology at the University of Dundee
Hunter, B. (Investigator), Lilley, D. (Investigator), Owen-Hughes, T. (Investigator), Wyatt, P. (Investigator) & van Aalten, D. (Investigator)
1/03/12 → 28/02/17
Project: Research