The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs). © 2010 Springer Basel AG.
CITATION STYLE
Pedone, E., Limauro, D., D’Ambrosio, K., De Simone, G., & Bartolucci, S. (2010, November). Multiple catalytically active thioredoxin folds: A winning strategy for many functions. Cellular and Molecular Life Sciences. https://doi.org/10.1007/s00018-010-0449-9
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