The 26 S proteasome in Entamoeba histolytica: divergence of the substrate binding pockets from host proteasomes.

ABSTRACT:

Objective

Proteasomes are conserved proteases crucial for proteostasis in eukaryotes and are promising drug targets for protozoan parasites. Yet, the proteasomes of Entamoeba histolytica remain understudied. The study's objective was to analyse the differences in the substrate binding pockets of amoeba proteasomes from those of host, and computational modelling of β5 catalytic subunit, with the goal of finding selective inhibitors.

Results

Comparative sequence analysis revealed differences in substrate binding sites of E. histolytica proteasomes, especially in the S1 and S3 pockets of the catalytic beta subunits, implying differences in substrate preference and susceptibility to inhibitors from host proteasomes. This was strongly supported by significantly lower sensitivity

SUBMITTER: Joshi N 

PROVIDER: S-EPMC11295364 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature