Article
The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin.
Structure (London, England : 1993) - 15 Jun 1994
Qin J, Clore G M, Gronenborn A M
Abstract excerpt
BACKGROUND: Thioredoxin is a ubiquitous protein and is involved in a variety of fundamental biological functions. Its active site is conserved and has two redox active cysteines in the sequence Trp-Cys-Gly-Pro-Cys. No structures of the oxidized and reduced states from the same species have been determined at high resolution under the same conditions and using the same methods. Hence, any detailed comparison of...
Topics
- Amino Acid Sequence
- Humans
- Hydrogen Bonding
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Molecular Structure
- Mutation
- Oxidation-Reduction
- Structure-Activity Relationship
- Thioredoxins
- Water