The FKBP s, or FK506 binding proteins, constitute a family of proteins that have prolyl isomerase activity and are related to the cyclophilins in function, though not in amino acid sequence. [1] .

FK506 binding proteins (FKBPs) are a family of highly conserved proteins in eukaryotes. The prototype of this protein family, FKBP12, is the binding partner for immunosuppressive drugs FK506 and rapamycin. FKBP12 functions as a cis/trans peptidyl prolyl isomerase (PPIase) that catalyzes interconversion between prolyl cis/trans conformations.

2021年11月18日 · FK506-binding proteins (FKBPs) belong to the immunophilin family. Like other immunophilins many FKBPs possess a cis-trans peptidyl-prolyl isomerase (PPIase) activity. In addition, they can act as a co-receptor for the natural products FK506 and Rapamycin.

FK506 binding protein 5, also known as FKBP5, is a protein which in humans is encoded by the FKBP5 gene. [5] The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking.

2011年8月1日 · FKBPs participate in cancer cellular processes. FKBPs are implicated in cell growth and survival and apoptotic signaling pathways. FKBP51 provide a relevant tissue marker of chemo-sensitivities and radio-sensitivities. FKBP52 autoantibodies are promising diagnostic cancer biomarkers.

2018年1月1日 · FKBP (FK506 Binding Protein), Table 1 FKBP classification with synonyms of gene and protein. In the 1970s, after a decade from the purification of cyclosporine, a selective immunosuppressant agent and potent tool in transplantation medicine, a novel molecule was purified from bacteria Streptomyces tsukubaensis.

FK506 binding (FKBP) proteins are part of the highly conserved immunophilin family and its members have fundamental roles in the regulation of signalling pathways involved in inflammation, adaptive immune responses, cancer and developmental biology.

2005年3月9日 · To probe the affinities involved in the formation of the FKBP·rapamycin·FRB complex, we used fluorescence polarization, surface plasmon resonance, and NMR spectroscopy. Analysis of the data shows that rapamycin binds to FRB with moderate affinity (Kd = 26 ± 0.8 μM).

Using structure-based design and protein mutagenesis we have remodeled the FKBP12 ligand binding site to include a sizable, hydrophobic specificity pocket.

2018年12月4日 · FK506-binding proteins (FKBPs) belong to the immunophilin family. Like other immunophilins many FKBPs possess a cis-trans peptidyl-prolyl isomerase (PPIase) activity. In addition, they can act as a co-receptor for the natural products FK506 and Rapamycin.