Article
The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin.
Biochemistry - 17 May 1994
Fejzo J, Etzkorn F A, Clubb R T, Shi Y, Walsh C T, Wagner G
Abstract excerpt
The periplasmic Escherichia coli cyclophilin is distantly related to human cyclophilin (34% sequence identity). Peptidyl-prolyl isomerase activity, cyclosporin A binding, and inhibition of the calcium-dependent phosphatase calcineurin are compared for human and E. coli wild-type and mutant proteins. Like human cyclophilin, the E. coli protein is a cis-trans peptidyl-prolyl isomerase. However, while the human...
Topics
- Amino Acid Isomerases
- Amino Acid Sequence
- Binding Sites
- Carrier Proteins
- Cyclosporine
- Escherichia coli
- Humans
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Peptidylprolyl Isomerase