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© Research
Publication : Biochemical and biophysical research communications

The ABP-120 C-end region from Entamoeba histolytica interacts with sulfatide, a new lipid target

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemical and biophysical research communications - 02 Nov 2005

Díaz-Valencia JD, Almaraz-Barrera Mde J, Arias-Romero LE, Hernandez-Rivas R, Rojo-Domínguez A, Guillén N, Vargas M

Link to Pubmed [PMID] – 16274663

Biochem. Biophys. Res. Commun. 2005 Dec;338(3):1527-36

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.

http://www.ncbi.nlm.nih.gov/pubmed/16274663