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...
Topics
- Amino Acid Sequence
- Binding Sites
- Crystallization
- Crystallography, X-Ray
- Cysteine
- Disulfides
- Dithiothreitol
- Humans
- Hydrogen Bonding
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Sequence Alignment
- Serine