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Crystallographic structure of glyceraldehyde-3-phosphate dehydrogenase from Schistosoma mansoniCrystallographic structure of glyceraldehyde-3-phosphate dehydrogenase from Schistosoma mansoni
Structural highlights
FunctionG3P_SCHMA This antigen is associated with human resistance to schistosomiasis. Publication Abstract from PubMedThe 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. Structure determination and analyses of the GAPDH from the parasite Schistosoma mansoni, the first one from a platyhelminth.,Boreiko S, Silva M, Iulek J Biochimie. 2021 May;184:18-25. doi: 10.1016/j.biochi.2021.01.014. Epub 2021 Jan , 30. PMID:33524435[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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