Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue*
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چکیده
The thioredoxin fold is the core scaffold of numerous proteins that control disulfide redox activity in the cell (1–3). These redox proteins share very little sequence homology, but all of them incorporate the four-stranded -sheet, three flanking -helices, and the redox-active CXXC motif of the TRX5 fold (Fig. 1A). The archetype of the family is thioredoxin (4), a disulfide reductase thatmaintains a reducing cytosolic environment. Other TRX fold redox proteins include the Dsb proteins (1), which regulate the formation of disulfide bonds in prokaryotes, and protein-disulfide isomerase (5), which catalyzes the oxida-
منابع مشابه
Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue*S⃞
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adj...
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تاریخ انتشار 2009