Understanding the architecture of human redox-relay complexes

Peroxiredoxins (Prdxs) are the major H2O2 scavengers in cells. Initially, Prdxs were only described as peroxidases, but lately they have been shown to transfer H2O2-derived oxidative equivalents via transient protein-protein interactions to target proteins, modulating their activity. This function is known as redox-relay.

Until now, there is no information about the structural aspects that determine the redox-relay functionality of Prdxs. In this project, I focus on the redox-relay between peroxiredoxin 2 (Prdx2) and the core-fragment (136-689 a.a.) of the transcription factor STAT3 (CF-STAT3) which occurs in the presence of a facilitator protein annexin A2 (AnxA2). I will mainly use cryogenic electron microscopy to study the structural organization of the Prdx2:CF-STAT3:AnxA2 complex to fully understand the mechanism of Prdx2 redox-relay.