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We propose that the requirement of two distinct glutathione interaction sites for the efficient reduction of glutathionylated disulfide substrates explains the deviating structurefunction relationships, activities and substrate preferences of different glutaredoxin subfamilies as well as thioredoxins

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Biomedical Chromatography 30 (2016) 1556-1572

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First, by interacting with the ECD region of TAS1R2, and second, by strengthening the hydrophobic interactions between the two lobes of ECD and lowering the free energy needed for their closure (Zhang et al., 2010)