Ab initio Structural Insights and Functional Analysis of Thioredoxin Glutathione Reductase from Schistosoma japonicum

Ab initio Structural Insights and Functional Analysis of Thioredoxin Glutathione Reductase from Schistosoma japonicum

Platyhelminth parasites are a major health problem in developing countries. Around the world Schistosomiasis remains a major public health concern affecting billions of people. In Schistosoma japonicum and some other platyhelminths Thioredoxin glutathione reductase (TGR) enzymes have been identified as alternative drug targets a key enzyme in the pathway of the parasite for detoxification of reactive oxygen species. In Thioredoxin glutathione reductase a C-terminal redox center containing selenocysteine (Sec) is present TGR is a homodimeric enzyme comprising a glutaredoxin domain and thioredoxin reductase (TR) domains. The secondary structural prediction of Thioredoxin glutathione reductase from Schistosoma japonicum has been done which would be useful for further analysis of this enzyme. Studies on annotating and analysing the function of (TGR) enzymes is done by using different bioinformatics tools like GRAVY, CELLO v.2.5, and by using different expasy tools. PDB-sum a web based tools is used to analyse insights of the enzyme TGR. For treatment of human schistosomiasis praziquantel is the only drug of choice. The emergence of drug resistance to praziquantel in schistosomes makes the development of novel drugs an urgent task. The present study is designed to analyse the ab initio structural and functional insights of the TGR as a target for development of novel antischistosomal agents in Schistosoma japonicum, a platyhelminth endemic in Asia.. .