Copper, a redox active metal, is a vital trace element required by all living organisms⁴ .  In biological systems, copper exists in two oxidation states, Cu(II) and Cu(I). The availability of these interchangeable states makes copper an effective redox-active metal, which is utilized by oxygen-dependent living organisms. Copper can also act as a critical cofactor for enzymes ¹ .

In human cells, copper concentrations are regulated via control of the levels of the copper transporter 1 (Ctr1) at the plasma membrane. In addition, the metallochaperone (Atox1) traffics copper to the ATP7A and ATP/7B, Cu-transporting P-type ATPases, which on copper-loading are translocated from the trans-golgi network to vesicles and/or the plasma membrane for copper export.

Human glutharedoxin-1 (hGrx1) is a cytosolic thiol disulfide oxidoreductase, which regulates the redox status of protein thiols ². A very recent study has demonstrated that hGrx1 interacts with the copper chaperone Atox1³. Our aim is to structurally characterize the hGrx1 protein and its interactions with protein partners such as Atox1, ATP7A and ATP7B. Progress towards this aim will be presented.