M. Paulino et al., MODELING A 3D STRUCTURE FOR EGDF1 FROM ECHINOCOCCUS-GRANULOSUS - PUTATIVE EPITOPES, PHOSPHORYLATION MOTIFS AND LIGAND, Journal of computer-aided molecular design, 12(4), 1998, pp. 351-360
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.