Binding Proteins FKBPs

FKBP12 (FKBP1A, 11950 Da) P62942, NP 463460 FK506-binding prot.lA 

FKBP12.6 (FKBP1B, 11782 Da) P68106, NP 004107 FK506-binding prot.lB 

FKBP15.9 (FKBP1C, 15903Da) NP 001011510 FK506-binding prot.lC 

FKBP15.6 (FKBP2,15649 Da) P26885, NP 476433 FK506-binding prot.2. FKBP13 

FKBP22 (FKBP11, 22180 Da) Q9NYL4, NP 057678 FK506-binding prot.11, FKBP19 

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FK-506 binding protein (FKBP) iigand, FK-506 binding protein (FKBP) iigand. 

Wulfing, C., Lombardero, J. and Pluckthun, A. (1994) An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. Journal of Biological Chemistry 269, 2895-2901. 

With another immunophilin, FK binding protein (FKBP), experiments were performed using isotope editing of the [U-13C]-labeled inhibitor ascomycin (bound to unlabeled FKBP) [34], as well as by isotope filtering with unlabeled ascomycin derivatives (bound to labeled FKBP) [35],... 

Tacrolimus (FK 506) is an immunosuppressant macrolide antibiotic produced by Streptomyces tsukubaensis. It is not chemically related to cyclosporine, but their mechanisms of action are similar. Both drugs bind to cytoplasmic peptidyl-prolyl isomerases that are abundant in all tissues. While cyclosporine binds to cyclophilin, tacrolimus binds to the immunophilin FK-binding protein (FKBP). Both complexes inhibit calcineurin, which is necessary for the activation of the T-cell-specific transcription factor NF-AT. 

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

The experimental determination of Aff and AS sometimes yields surprising results, as, for example, in the thermodynamics of hydrogen-bond formation in the complex of FK506 or rapamycin with FK506-binding protein (FKBP). " Binding to the wild-type and to the mutant Tyr 82 Phe 82 was... 

There are several examples that illustrate the potential of SAR by NMR. As noted earlier, FK506 binding protein (FKBP) inhibits cal-cineurin and blocks T-cell activation when complexedtothe immunosuppressant FK506. This protein was used as a target for SAR by... 

These observations in turn led to the observation of noncovalent protein complexes. The noncovalent binding between the immunosuppressive binding protein FKBP and the iimnunosuppressive agents FK506 and rapamycin, probed by electrospray MS, was reported by Ganem et al. [72] in 1991. This report and the next one on enzyme-substrate interactions with hen egg-white lysozyme [73] attracted considerable attention. The study of noncovalent interactions by ESI-MS... 

Fischer, S., Michnick, S. and Karplus, M. (1993) A Mechanism for Rotamase Catalysis by the FK506 Binding Protein (FKBP), Biochemistry 32, 13830-13837. 

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