High impact information on FK506-bp2

• FKBP12 binds to ligand-free TGF beta type I receptor, from which it is released upon a ligand-induced, type II receptor mediated phosphorylation of the type I receptor [1].
• The immunophilins cyclophilin and FK506 binding protein (FKBP) are small, predominantly soluble proteins that bind the immunosuppressant drugs cyclosporin A and FK506, respectively, with high affinity, and which seem to mediate their pharmacological actions [2].
• Antisense experiments revealed that the so observed regulation of the FK506-binding protein, FKBP38, plays a role in TSC gene-dependent cell size regulation [3].
• The shut-down gene of Drosophila melanogaster encodes a novel FK506-binding protein essential for the formation of germline cysts during oogenesis [4].
• A Drosophila cDNA encoding a structural homolog of mammalian FKBP59 (also identified as FKBP52), a member of the FK506-binding protein (FKBP) class of immunophilins, was isolated [5].

Biological context of FK506-bp2

• The third group of PPIases encoded in the genome comprises two proteins (hPin1 and hParv14) where hPin1 is an important PPIase for cell cycle [6].
• The predicted amino acid sequence of this cDNA shows that the dFKBP59 protein contains one highly conserved FKBP12-like domain followed by two others with less conservation [5].

Analytical, diagnostic and therapeutic context of FK506-bp2

• Molecular cloning and embryonic expression of dFKBP59, a novel Drosophila FK506-binding protein [5].

References