Download MendeleyThe solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.
Qin, J., Clore, G.M., Kennedy, W.P., Kuszewski, J., Gronenborn, A.M.(1996) Structure 4: 613-620
- PubMed: 8736558
- DOI: https://doi.org/10.1016/s0969-2126(96)00065-2
- Primary Citation of Related Structures:
1CQG, 1CQH - PubMed Abstract:
Human thioredoxin (hTRX) is a 12 kDa cellular redox protein that has been shown to play an important role in the activation of a number of transcriptional and translational regulators via a thiol-redox mechanism. This activity may be direct or indirect via another redox protein known as Ref-1. The structure of a complex of hTRX with a peptide comprising its target from the transcription factor NF kappa B has previously been solved. To further extend our knowledge of the recognition by and interaction of hTRX with its various targets, we have studied a complex between hTRX and a Ref-1 peptide. This complex represents 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.
