Title: Insights into Immunophilin Structure and Function
VOLUME: 18 ISSUE: 35
Author(s):C. Lucke and M. Weiwad
Affiliation:Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany.
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.
