Article
The CXC motif: a functional mimic of protein disulfide isomerase.
Biochemistry - 13 May 2003
Woycechowsky Kenneth J, Raines Ronald T
Abstract excerpt
Protein disulfide isomerase (PDI) utilizes the active site sequence Cys-Gly-His-Cys (CGHC; E degrees ' = -180 mV) to effect thiol-disulfide interchange during oxidative protein folding. Here, the Cys-Gly-Cys-NH(2) (CGC) peptide is shown to have a disulfide reduction potential (E degrees ' = -167 mV) that is close to that of PDI. This peptide has a thiol acid dissociation constant (pK(a) = 8.7) that is lower than...
Topics
- Amino Acid Motifs
- Binding Sites
- Cysteine
- Disulfides
- Escherichia coli
- Genetic Vectors
- Kinetics
- Molecular Mimicry
- Mutation
- NADP
- Oxidation-Reduction
- Protein Conformation
- Protein Disulfide-Isomerases
- Protein Folding
- Spectrometry, Fluorescence
- Substrate Specificity
- Sulfhydryl Compounds
- Thioredoxin-Disulfide Reductase