Abstract
FK506 binding proteins (FKBPs) are a family of highly conserved proteins in eukaryotes. The prototype of this protein family, FKBP12, is the binding partner for immunosuppressive drugs FK506 and rapamycin. FKBP12 functions as a cis/trans peptidyl prolyl isomerase (PPIase) that catalyzes interconversion between prolyl cis/trans conformations. Members of the FKBP family contain one or several PPIase domains, which do not always exhibit PPIase activity yet are all essential for their function. FKBPs are involved in diverse cellular functions including protein folding, cellular signaling, apoptosis and transcription. They elicit their function through direct binding and altering conformation of their target proteins, hence acting as molecular switches. In this review, we provide a general summary for the structures and diverse functions of FKBPs found in mammalian cells.
Keywords: Calcineurin, FK506, FK506 binding proteins, immunophilin, mTOR, peptidyl prolyl cis/trans isomerase.
Current Molecular Pharmacology
Title:FK506-Binding Proteins and Their Diverse Functions
Volume: 9
Author(s): Mingming Tong and Yu Jiang
Affiliation:
Keywords: Calcineurin, FK506, FK506 binding proteins, immunophilin, mTOR, peptidyl prolyl cis/trans isomerase.
Abstract: FK506 binding proteins (FKBPs) are a family of highly conserved proteins in eukaryotes. The prototype of this protein family, FKBP12, is the binding partner for immunosuppressive drugs FK506 and rapamycin. FKBP12 functions as a cis/trans peptidyl prolyl isomerase (PPIase) that catalyzes interconversion between prolyl cis/trans conformations. Members of the FKBP family contain one or several PPIase domains, which do not always exhibit PPIase activity yet are all essential for their function. FKBPs are involved in diverse cellular functions including protein folding, cellular signaling, apoptosis and transcription. They elicit their function through direct binding and altering conformation of their target proteins, hence acting as molecular switches. In this review, we provide a general summary for the structures and diverse functions of FKBPs found in mammalian cells.
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Cite this article as:
Tong Mingming and Jiang Yu, FK506-Binding Proteins and Their Diverse Functions, Current Molecular Pharmacology 2016; 9 (1) . https://dx.doi.org/10.2174/1874467208666150519113541
DOI https://dx.doi.org/10.2174/1874467208666150519113541 |
Print ISSN 1874-4672 |
Publisher Name Bentham Science Publisher |
Online ISSN 1874-4702 |
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