Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.
Qin, J., Clore, G.M., Kennedy, W.M., Huth, J.R., Gronenborn, A.M.(1995) Structure 3: 289-297
- PubMed: 7788295 
- DOI: https://doi.org/10.1016/s0969-2126(01)00159-9
- Primary Citation of Related Structures:  
1MDI, 1MDJ, 1MDK - PubMed Abstract: 
Human thioredoxin is a 12 kDa cellular redox protein that plays a key role in maintaining the redox environment of the cell. It has recently been shown to be responsible for activating the DNA-binding properties of the cellular transcription factor, NF kappa B, by reducing a disulfide bond involving Cys62 of the p50 subunit. Using multidimensional heteronuclear-edited and hetero-nuclear-filtered NMR spectroscopy, we have solved the solution structure of a complex of human thioredoxin and a 13-residue peptide extending from residues 56-68 of p50, representing a kinetically stable mixed disulfide intermediate along the reaction pathway.
Organizational Affiliation: 
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.