Two structures of cyclophilin 40: folding and fidelity in the TPR domains.
Taylor, P., Dornan, J., Carrello, A., Minchin, R.F., Ratajczak, T., Walkinshaw, M.D.(2001) Structure 9: 431-438
- PubMed: 11377203 
- DOI: https://doi.org/10.1016/s0969-2126(01)00603-7
- Primary Citation of Related Structures:  
1IHG, 1IIP - PubMed Abstract: 
The "large immunophilin" family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity.
Organizational Affiliation: 
Structural Biochemistry Group, Institute of Cell and Molecular Biology, The University of Edinburgh, Michael Swann Building, King's Buildings, Mayfield Road, EH9 3JR, Edinburgh, United Kingdom.