FK506-binding protein 1A F36V mutant domain-containing fusion protein (FKBP1A(F36V) fusion protein)

The FK506-binding protein 1A F36V mutant domain-containing fusion protein is a synthetic, engineered protein designed for precise, ligand-inducible control in cellular and gene therapy applications. The F36V point mutation in the FKBP1A (also called FKBP12) domain creates an enlarged specificity pocket that selectively binds to synthetic small-molecule ligands—such as AP1903 (rimiducid) or Shield-1—with nanomolar affinity, but not to wild-type FKBP-targeting drugs like FK506 or rapamycin[1][3][4]. When fused to signaling, regulatory, or effector protein domains (such as the intracellular portion of the Fas receptor or destabilization domains), administration of the small-molecule ligand triggers dimerization, activation, or stabilization of the fusion protein in a highly controlled, reversible, and modular fashion[4]. This system is especially useful for chemically controlled regulation of cell fate (e.g., engineered T cell ablation via induced apoptosis) or for conditional protein degradation/stabilization in research and therapeutic contexts[3][4]. The use of the F36V mutant domain ensures that the ligand acts specifically on engineered cells expressing the fusion protein, minimizing off-target effects on endogenous FKBP proteins[1][4].

Other names

FKBP12-F36V fusion proteinFKBP1A F36V mutant fusion proteinFKBP F36V domain fusion proteinDmrA fusion protein (note: sometimes DmrA used in commercial systems)

Synthetic ligand binding to the F36V-mutant cavity induces dimerization or stabilization of the fusion protein, enabling/executing downstream biological effects controlled by fusion domain context (e.g., apoptosis by Fas domain fusion, stabilization/destabilization of target protein)[1][3][4].