Background: Thioredoxin is a physiological inhibitor of ASK1. Results: The catalytic motif of thioredoxin is essential for its binding to ASK1 and the interaction does not involve intermolecular disulfide bonds. Conclusion: Thioredoxin-binding domain of ASK1 is a rigid domain that interacts with reduced thioredoxin through a large binding interface. Significance: Structural basis of the interaction between ASK1 and reduced thioredoxin.
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