| Autor: |
Pavão F; Instituto de Química de São Carlos, USP, São Carlos, SP, Brazil., Castilho MS, Pupo MT, Dias RL, Correa AG, Fernandes JB, da Silva MF, Mafezoli J, Vieira PC, Oliva G |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 2002 Jun 05; Vol. 520 (1-3), pp. 13-7. |
| DOI: |
10.1016/s0014-5793(02)02700-x |
| Abstrakt: |
The structure of the glycosomal glyceraldehyde-3-phosphate dehydrogenase (gGAPDH) from Trypanosoma cruzi complexed with chalepin, a natural product from Pilocarpus spicatus, has been determined by X-ray crystallography to 1.95 A resolution. The structure is in the apo form without cofactors in the subunits of the tetrameric gGAPDH in the asymmetric unit. Unequivocal density corresponding to the inhibitor was clearly identified in one monomer. The final refined model of the complex shows extensive conformational changes when compared with the native structure. The mode of binding of chalepin to gGAPDH and its implications for inhibitor design are discussed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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