Journal:Acta Cryst D:S2059798324006594
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | Chagas disease is a neglected tropical disease caused by the protozoan parasite Trypanosoma cruzi. The significant global health burden and limited treatment options call for the development of new and effective drugs. Recent research has identified certain metabolic enzymes as promising targets for drug development. Among these, glycerol kinase (GK), a key enzyme in glycerol metabolism, has drawn attention due to its potential role in the parasite’s survival and proliferation. | + | Chagas disease is a neglected tropical disease caused by the protozoan parasite ''Trypanosoma cruzi''. The significant global health burden and limited treatment options call for the development of new and effective drugs. Recent research has identified certain metabolic enzymes as promising targets for drug development. Among these, glycerol kinase (GK), a key enzyme in glycerol metabolism, has drawn attention due to its potential role in the parasite’s survival and proliferation. |
In our study, we have elucidated the crystal structure of GK from T. cruzi, providing critical insights into its function and potential as a drug target. Through comparative sequence analysis, we explored the evolutionary conservation and unique features of this enzyme, which set the stage for a deeper understanding of its role in the parasite's metabolism. Structural analysis allowed a detailed description of the glycerol binding pocket, while superimposition with GK structure from closely related Trypanosoma brucei revealed a strategic location for ATP binding. Notably, the overall fold of the structure, including the dimerization interface, was characterized, highlighting regions crucial for the enzyme's stability and function. | In our study, we have elucidated the crystal structure of GK from T. cruzi, providing critical insights into its function and potential as a drug target. Through comparative sequence analysis, we explored the evolutionary conservation and unique features of this enzyme, which set the stage for a deeper understanding of its role in the parasite's metabolism. Structural analysis allowed a detailed description of the glycerol binding pocket, while superimposition with GK structure from closely related Trypanosoma brucei revealed a strategic location for ATP binding. Notably, the overall fold of the structure, including the dimerization interface, was characterized, highlighting regions crucial for the enzyme's stability and function. | ||
Revision as of 12:45, 13 July 2024
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