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What is FK506 binding protein?

What is FK506 binding protein?

FK506 binding proteins (FKBPs) are a large family of proteins that possess peptidyl prolyl cis/trans isomerase (PPIase) domains. The founding member of this family is FKBP12, which is a 108 amino acid peptide containing the minimal sequence for a PPIase [1, 2].

What does FK506 do?

FKBPs are involved in diverse cellular functions including protein folding, cellular signaling, apoptosis and transcription. They elicit their function through direct binding and altering conformation of their target proteins, hence acting as molecular switches.

What does the FKBP5 gene do?

The FKBP5 gene encodes a molecular co-chaperone of the glucocorticoid receptor complex, which modulates intracellular glucocorticoid signaling and plays an important role in homeostatic regulation of the stress response [42].

What is FRB protein?

FRB is a small domain derived from full length mTOR. In brief, rapamycin binds to a protein called FKBP12. Rapamycin bound to FKBP12 inhibits mTOR signaling. For your Materials & Methods section: pEGFP-FRB was a gift from Klaus Hahn (Addgene plasmid # 25919 ; http://n2t.net/addgene:25919 ; RRID:Addgene_25919)

What is a FK506 level?

The mean FK506 whole-blood and plasma levels were 14.1 +/- 0.26 ng/ml and 0.96 +/- 0.75 ng/ml, respectively. There was a large intra- and interpatient variability in the ratio between whole-blood and plasma levels (range 1.0-73.5), with a mean ratio of 18.0 +/- 0.28 (+/- SEM).

How does FK506 inhibit calcineurin?

FK506 (Tacrolimus) is commonly used as an immunosuppressant to prevent the rejection of organ transplants. Similarly to cyclosporin A (CsA), FK506 blocks the activation of calcineurin through the formation of complexes with immunophilins.

What is FKBP5 methylation?

DNA methylation of the FKBP5 gene is assumed to alter FKBP5 expression and hence the synthesis of the FK506 binding protein 51, a central element of a genomic negative feedback loop for glucocorticoid receptor signaling.

FK506 binding proteins (FKBPs) are a large family of proteins that possess peptidyl prolyl cis/transisomerase (PPIase) domains. The founding member of this family is FKBP12, which is a 108 amino acid peptide containing the minimal sequence for a PPIase [1, 2].

Does PPIase bind to FK506?

The PPIase domain binds FK506 weakly in vitro. FKBP19 is highly expressed in the tumor tissue of hepatocellular carcinoma, suggesting that it may play a role in hepatic tumor development [144]. The other members of the ER FKBPs all contain two EF-hand motifs that bind to Ca2+.

Does fkbp23 bind to BIP in the ER?

[147] Zhang X; Wang Y; Li H; Zhang W; Wu D; Mi H, The mouse FKBP23 binds to BiP in ER and the binding of C-terminal domain is interrelated with Ca2+ concentration. FEBS letters2004, 559(1–3), 57–60. [PubMed] [Google Scholar]

What does FKBP51 mean in melanoma?

In melanomas FKBP51 expression correlates with the invasiveness and aggressiveness of the cancer [189]. It has been shown that FKBP51 exhibits anti-apoptosis activity and protects the cancer cells from irradiation induced cell death [127, 189].