FK506 binding proteins functions

The protein phosphatase calcineurin was of particular interest since it mediates the immunosuppressive effect of the pharmaceuticals cyclosporin and FK506, often used in organ and tissue transplantations. The biochemical point of application of both pharmaceuticals was unclear for a long time. In initial experiments, it was found that cyclosporin and FK506 bind specifically to two proteins known as cyclophilin and FK506 binding protein, respectively. Both proteins function as peptidyl prolyl cis/trans isome-rases (review Fischer, 1994). 

Brillantes, A.-M. B., Ondrias, K., Scott, A., Kobrinsky, E., Ondriasova, E. et al. (1994). Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein. Cell77,513-23. 

Kay, J. E. (1996). Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases. Biochem.J. 314, 361-385. 

Yang, W. M.,Yao,Y. L., and Seto, E. (2001). The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YYl. EMBO J. 20,4814-4825. 

FKBP, or FK506 binding protein-a family of proteins related to the cyclophilins in function and exhibits a prolyl isomer-ase activity see Siekierka JJ, Hung SH, Poe M, Lin CS, Sigal NH. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 1989 341 (6244) 755-757. 

FK506 (tacrolimus)/ rni binding to proteins it serves to unravel cell trafficking and protein function Haggarty 2000... 

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