1. The ABP-120 C-end region from Entamoeba histolytica interacts with sulfatide, a new lipid target.
- Author
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Díaz-Valencia JD, Almaraz-Barrera Mde J, Arias-Romero LE, Hernandez-Rivas R, Rojo-Domínguez A, Guillén N, and Vargas M
- Subjects
- Amino Acid Sequence, Animals, Cell Membrane chemistry, Cell Membrane genetics, Cell Membrane metabolism, Contractile Proteins genetics, Entamoeba histolytica genetics, Filamins, Microfilament Proteins genetics, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Alignment, Substrate Specificity, Transfection, Contractile Proteins chemistry, Contractile Proteins metabolism, Entamoeba histolytica metabolism, Microfilament Proteins chemistry, Microfilament Proteins metabolism, Sulfoglycosphingolipids metabolism
- Abstract
EhABP-120 is the first filamin identified in the parasitic protozoan Entamoeba histolytica. Filamins are a family of cross-linking actin-binding proteins that promote a dynamic orthogonal web. They have been reported to interact directly with more than 30 cellular proteins and some phosphoinositides. The biochemical consequences of these interactions may have either positive or negative effects on the cross-linking function and also form a link between the cytoskeleton and plasma membrane. In this study, the EhABP-120 carboxy-terminal domain (END) was biochemically characterized. This domain was able to associate to 3-sulfate galactosyl ceramide, a new lipid target for a member of the filamin family. Also, the END domain was able to dimerize "in vitro." Molecular modeling analysis showed that the dimeric region is stabilized by a disulfide bond. Electrostatic and docking studies suggest that an electropositive concave pocket at the dimeric END domain interacts simultaneously with several sulfogalactose moieties of the sulfatide. more...
- Published
- 2005
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