New insights on human IRE1 tetramer structures based on molecular modeling.

ABSTRACT: Inositol-Requiring Enzyme 1α (IRE1α; hereafter IRE1) is a transmembrane kinase/ribonuclease protein related with the unfolded protein response (UPR) signaling. Experimental evidence suggests that IRE1 forms several three dimensional (3D) structural variants: dimers, tetramers and higher order oligomers, where each structural variant can contain different IRE1 conformers in different arrangements. For example, studies have shown that two sets of IRE1 dimers exist; a face-to-face dimer and a back-to-back dimer, with the latter considered the important unit for UPR signaling propagation. However, the structural configuration and mechanistic details of the biologically important IRE1 tetramers are limited. Here, we combine protein-protein docking with molecular dynamics simulations to derive h

SUBMITTER: Carlesso A 

PROVIDER: S-EPMC7567888 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature