Article
Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.
Structure (London, England : 1993) - 15 Jun 1996
Weichsel A, Gasdaska J R, Powis G, Montfort W R
Abstract excerpt
BACKGROUND: Human thioredoxin reduces the disulfide bonds of numerous proteins in vitro, and can activate transcription factors such as NFkB in vivo. Thioredoxin can also act as a growth factor, and is overexpressed and secreted in certain tumor cells. RESULTS: Crystal structures were determined for reduced and oxidized wild type human thioredoxin (at 1.7 and 2.1 A nominal resolution, respectively), and for...
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