Structural and functional characterization of the divergent Entamoeba Src using Src inhibitor-1.

ABSTRACT:

Background

The abundant number of kinases that Entamoeba histolytica possesses allows us to assume that the regulation of cellular functions by phosphorylation-dephosphorylation processes is very important. However, the kinases responsible for the phosphorylation in Entamoeba spp. vary in the structure of their domains and, therefore, could be responsible for the unusual biological characteristics of this parasite. In higher eukaryotes, Src kinases share conserved structural domains and are very important in the regulation of the actin cytoskeleton. In both Entamoeba histolytica and Entamoeba invadens, the major Src kinase homologue of higher eukaryotes lacks SH3 and SH2 domains, but does have KELCH domains; the latter are part of actin cross-linking proteins in higher eukaryotic c

SUBMITTER: Lopez-Contreras L 

PROVIDER: S-EPMC5648430 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature