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A conformational-dependent interdomain redox relay at the core of Protein Disulfide Isomerase activity.

Eduardo José Xavier Rodrigues Pinho MeloSoukaina El-GuendouzCatia CorreiaFernando TeodoroCarlos LopesPaulo J Martel
Published in: Antioxidants & redox signaling (2024)
The two active sites of PDIA1 work cooperatively as an interdomain redox relay mechanism that explains PDIA1 oxidative activity to form native disulfides and PDIA1 reductase activity to resolve scrambled disulfides. This mechanism suggests a new rationale for shutting down oxidative protein folding under ER redox imbalance. Whether it applies to physiological substrates in cells remains to be shown.
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