MODELING A 3D STRUCTURE FOR EGDF1 FROM ECHINOCOCCUS-GRANULOSUS - PUTATIVE EPITOPES, PHOSPHORYLATION MOTIFS AND LIGAND

EgDf1 is a developmentally regulated protein from the parasite Echinoc occus granulosus related to a family of hydrophobic ligand binding pro teins, This protein could play a crucial role during the parasite life cycle development since this organism is unable to synthetize most of their own lipids de novo, Furthermore, it has been shown that two rel ated protein from other parasitic platyhelminths (Fh15 from Fasciola h epatica and Sm14 from Schistosoma mansoni) are able to confer protecti ve inmunity against experimental infection in animal models. A three-d imensional structure would help establishing structure/function relati onships on a knowledge based manner. 3D structures for EgDf1 protein w ere modelled by using myelin P2 (mP2) and intestine fatty acid binding protein (I-FABP) as templates. Molecular dynamics techniques were use d to validate the models. Template mP2 yielded the best 3D structure f or EgDf1. Palmitic and oleic acids were docked inside EgDf1. The prese nt theoretical results suggest definite location in the secondary stru cture of the epitopic regions, consensus phosphorylation motifs and ol eic acid as a good ligand candidate to EgDf1. This protein might well be involved in the process of supplying hydrophobic metabolites for me mbrane biosynthesis and for signaling pathways.