Abstract
The immunophilins are proteins which are capable of influencing the immune response in combination with an immunosuppressive drug. Their natural function, however, is mainly the cis/trans isomerization of peptidyl-prolyl bonds in other proteins. This review lists all immunophilin structure coordinates currently available in the RCSB protein data bank and highlights the key active-site factors that define their catalytic and immunological action. In addition, an overview of biologically-relevant functions is provided for various immunophilin members.
Keywords: Calcineurin, cyclophilin, FK506-binding protein, immunophilin, immunosuppression, PPIase domain, peptidyl-prolyl bonds, topology, hydrophobic cyclic, hydrophobic macrolides
Current Medicinal Chemistry
Title: Insights into Immunophilin Structure and Function
Volume: 18 Issue: 35
Author(s): C. Lucke and M. Weiwad
Affiliation:
Keywords: Calcineurin, cyclophilin, FK506-binding protein, immunophilin, immunosuppression, PPIase domain, peptidyl-prolyl bonds, topology, hydrophobic cyclic, hydrophobic macrolides
Abstract: The immunophilins are proteins which are capable of influencing the immune response in combination with an immunosuppressive drug. Their natural function, however, is mainly the cis/trans isomerization of peptidyl-prolyl bonds in other proteins. This review lists all immunophilin structure coordinates currently available in the RCSB protein data bank and highlights the key active-site factors that define their catalytic and immunological action. In addition, an overview of biologically-relevant functions is provided for various immunophilin members.
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Cite this article as:
Lucke C. and Weiwad M., Insights into Immunophilin Structure and Function, Current Medicinal Chemistry 2011; 18 (35) . https://dx.doi.org/10.2174/092986711798194324
DOI https://dx.doi.org/10.2174/092986711798194324 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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