Cellular and Molecular Life Sciences CMLS

, Volume 63, Issue 24, pp 2889–2900 | Cite as

Immunophilins: for the love of proteins

  • S. Barik


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.


Immunophilin PPIase chaperone cyclophilin (Cyp) FK506-binding protein (FK506) trigger factor TPR domain dual-family immunophilin protein folding 


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Copyright information

© Birkhäuser Verlag, Basel 2006

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular Biology (MSB 2370)University of South Alabama, College of MedicineMobileUSA

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