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Current Molecular Pharmacology

Editor-in-Chief

ISSN (Print): 1874-4672
ISSN (Online): 1874-4702

Immunophilins: Structures, Mechanisms and Ligands

Author(s): Amaravadhi Harikishore and Ho Sup Yoon

Volume 9, Issue 1, 2016

Page: [37 - 47] Pages: 11

DOI: 10.2174/1874467208666150519113427

Price: $65

Abstract

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.

Graphical Abstract

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