Abstract.
Immunophilins are chaperones that may also exhibit peptidylprolyl isomerase (PPIase) activity. This review summarizes our knowledge of the two largest families of immunophilins, namely cyclophilin and FK506-binding protein, and a novel chimeric dual-family immunophilin, named FK506- and cyclosporin-binding protein (FCBP). The larger members of each family are modular in nature, consisting of multiple PPIase and/or protein-protein interaction domains. Despite the apparent difference in their sequence and three-dimensional structure, the three families encode similar enzymatic and biological functions. Recent studies have revealed that many immunophilins possess a chaperone function independent of PPIase activity. Knockout animal studies have confirmed multiple essential roles of immunophilins in physiology and development. An immunophilin is indeed a natural ‘protein-philin’ (Greek ‘philin’ = friend) that interacts with proteins to guide their proper folding and assembly.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Author information
Authors and Affiliations
Corresponding author
Additional information
Received: 7 May 2006; received after revision 3 July 2006; accepted 24 August 2006
Rights and permissions
About this article
Cite this article
Barik, S. Immunophilins: for the love of proteins. Cell. Mol. Life Sci. 63, 2889–2900 (2006). https://doi.org/10.1007/s00018-006-6215-3
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00018-006-6215-3