Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation
- 1 August 1997
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 271 (2) , 258-265
- https://doi.org/10.1006/jmbi.1997.1151
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- The Mutant Escherichia coli F112W Cyclophilin Binds Cyclosporin A in Nearly Identical Conformation as Human CyclophilinBiochemistry, 1994
- 15N NMR Relaxation Studies of the FK506 Binding Protein: Dynamic Effects of Ligand Binding and Implications for Calcineurin RecognitionBiochemistry, 1994
- Three-Dimensional Solution Structure of Escherichia coli Periplasmic CyclophilinBiochemistry, 1994
- Peptidylproline cis‐trans‐isomerases: immunophilinsEuropean Journal of Biochemistry, 1993
- Similarities and differences between human cyclophilin A and other β-barrel structures: Structural refinement at 1.63 Å resolutionJournal of Molecular Biology, 1992
- Structural and functional characterization of Escherichia coli peptidyl‐prolyl cis‐trans isomerasesEuropean Journal of Biochemistry, 1992
- The X‐ray structure of a tetrapeptide bound to the active site of human cyclophilin AFEBS Letters, 1992
- Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cellsBiochemistry, 1991
- Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteinsNature, 1989
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983