The researchers determined that the propeller - shaped ISRIB molecule fits snugly into a pocket deep inside eIF2B where it holds together two identical subcomplexes of the larger protein. (ucsf.edu)
The researchers saw that the propeller - shaped ISRIB sits deep inside eIF2B and acts as a molecular staple to pin two identical subcomplexes together. (sciencedaily.com)
The project focuses on the dynamics of transient microcompartments formed by the V - ATPase holoenzyme, V - ATPase subcomplexes and subunits together with the mentioned proteins, with the aim to understand the mechanisms leading to this unique type of physiologically relevant regulation. (biologie.uni-osnabrueck.de)