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Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Insights into Immunophilin Structure and Function

Author(s): C. Lucke and M. Weiwad

Volume 18 , Issue 35 , 2011

Page: [5333 - 5354] Pages: 22

DOI: 10.2174/092986711798194324

Price: $65

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


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