Immunophilins consist of a family of highly conserved proteins which possess binding
abilities to immunosuppressive drugs. Cyclophilins (Cyps) and FK506-binding proteins (FKBP) are
family proteins collectively referred as immunophilins. Most Cyps and FKBP family members catalyse
peptidyl-prolyl cis/trans isomerase (PPIase) mediated reactions and form binary complexes with
their ligands cyclosporine A and FK506. Immunophilins are also involved in key biochemical processes
including protein folding, receptor signalling, protein trafficking, and transcription and exhibit
versatile biological functions, when complexed with their ligands. Therapeutic implications of immunophilins and effects
of their ligands in neurodegenerative disorders, cancer, and infectious diseases have been accumulating in recent years.
This review focuses on molecular characteristics of the canonical and non-canonical immunophilin family members from
human and Plasmodium falciparum and P. vivax, recent progress on immunophilin inhibitor development, and future perspectives
of structure-based design of non-immunosuppressive immunophilin ligands with potential pharmacological activities
against infectious diseases.
Keywords: Cyclophilin, cyclosporine, calcineurin, FK506 binding protein (FKBP), FK506, immunophilins, PPIase, rapamycin.
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