Structure determination and analyses of the GAPDH from the parasite Schistosoma mansoni, the first one from a platyhelminth
| Autor: | Sheila Boreiko, Jorge Iulek, Marcio Silva |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular 0301 basic medicine Dehydrogenase Schistosomiasis Context (language use) Crystallography X-Ray Biochemistry 03 medical and health sciences medicine Animals Parasite hosting Glyceraldehyde 3-phosphate dehydrogenase chemistry.chemical_classification 030102 biochemistry & molecular biology biology Glyceraldehyde-3-Phosphate Dehydrogenases Helminth Proteins Schistosoma mansoni General Medicine biology.organism_classification medicine.disease 030104 developmental biology Enzyme chemistry biology.protein NAD+ kinase |
| Zdroj: | Biochimie. 184:18-25 |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/j.biochi.2021.01.014 |
| Popis: | The enzyme Glyceraldehyde-3-Phosphate Dehydrogenase from Schistosoma mansoni (SmGAPDH) is characterized as a therapeutical target for schistosomiasis. In this context, we report here the experimental structure, structural analyses and comparisons of SmGAPDH, the first one from a Platyhelminth. The enzyme was expressed, purified and assayed for crystallization, what allowed the obtainment of crystals of sufficient quality to collect X-ray diffraction data up to 2.51 A resolution. SmGAPDH is the only GAPDH to present the sequence NNR (its residues 114–116) which leads to (especially R116) a hydrogen bond network that possibly reflects on the flexibility of residues to interact with the adenine part of NAD+, speculated to be important for differential drug design. |
| Databáze: | OpenAIRE |
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