【摘 要】
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The term immunophilin involves a family of proteins whose domain shows peptidyl-prolyl-(cis/trans)-isomerase (PPIase) enzymatic activity, i.e., the reversible cis/trans interconversion of Xaa-Pro bonds (Annett et al., 2020). The PPIase domain of these pro
【机 构】
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Instituto de Biología y Medicina Experimental/CONICET&Departamento de Química Biológica,Facultad de
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The term immunophilin involves a family of proteins whose domain shows peptidyl-prolyl-(cis/trans)-isomerase (PPIase) enzymatic activity, i.e., the reversible cis/trans interconversion of Xaa-Pro bonds (Annett et al., 2020). The PPIase domain of these proteins usually binds to immunosuppressive drugs, such as the macrolide FK506 (referred to as the FKBP subfamily) or the cyclic undecapeptide cyclosporine A (called CyP subfamily). The binding of the drug implies the inhibition of the PPIase enzymatic activity. Those members of each subfamily that show the smallest molecular weight (i.e., FKBP12 and CyP17/CyPA) are the only proteins responsible for the immunosuppressive action of the cognate drug due to the abrogation of calcineurin (or protein-phosphatase 2B) biological action.
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