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Plasmodium falciparum is a causative agent of one of the most devastating disease, cerebral malaria. Absence of suitable vaccine and the emergence of multi drug resistant parasites hinder prevention of malaria disease worldwide. One of the most reliable approaches to control this disease is to develop antimalarial against drug targets which are specific for ubiquitous and necessary enzymes such as helicases. Helicases work in ATP dependent manner and help in unwinding of nucleic acids during replication, transcription and repair mechanism. In this study, in silico analysis and homology modeling method were used to characterize the physicochemical properties and 3D structure of PfBrr2 helicase. Suitable structure of different domains was validated using in silico tools and used for docking studies to understand proteinligand interactions. Protein-protein interaction network of PfBrr2 was investigated to understand its function inside the parasite.

In silico Structural Characterization of Plasmodium falciparum helicase, PfBrr2