FK506-binding protein F36V mutant domain (F36V-FKBP12)

The FK506-binding protein (FKBP) F36V mutant is a genetically engineered variant of the human FKBP12 protein, in which the phenylalanine at position 36 is replaced by valine. This mutation creates a unique, hydrophobic specificity pocket within the ligand-binding site of FKBP12, enabling selective binding to synthetic ligands that do not interact with wild-type FKBP12. It is widely used in chemical biology as part of dimerization systems. Synthetic ligands can induce or disrupt dimerization/fusion events involving proteins tagged with this mutant domain, enabling conditional control over signaling pathways or transcriptional activity. Ligand-induced recruitment of E3 ubiquitin ligases via fusion to an F36V-FKBP tag enables rapid degradation of target proteins.

Other names

FKBP12 F36V mutantF36V FKBPFKBP F36VFKBP12-F36V

Selective binding to synthetic ligands with "bumped" substituents, enabling conditional protein dimerization or degradation.