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Details on Person FK506 binding protein 5 (FKBP51, also known as FKBP5) is a m...
| Class:Id | Summation:8941425 |
|---|---|
| _displayName | FK506 binding protein 5 (FKBP51, also known as FKBP5) is a m... |
| _timestamp | 2017-02-22 17:49:08 |
| created | [InstanceEdit:8941426] Shamovsky, Veronica, 2016-09-30 |
| literatureReference | [LiteratureReference:8944722] FKBP family proteins: immunophilins with versatile biological functions [LiteratureReference:8937317] Steroid receptor interactions with heat shock protein and immunophilin chaperones [LiteratureReference:8944720] Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506 [LiteratureReference:8944723] The interchange of immunophilins leads to parallel pathways and different intermediates in the assembly of Hsp90 glucocorticoid receptor complexes [LiteratureReference:8936926] Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle |
| modified | [InstanceEdit:8944728] Shamovsky, Veronica, 2016-11-04 [InstanceEdit:8955051] Shamovsky, Veronica, 2017-01-10 [InstanceEdit:8979210] Shamovsky, Veronica, 2017-02-22 |
| text | FK506 binding protein 5 (FKBP51, also known as FKBP5) is a member of the immunophilin (IMM) protein family of intracellular proteins. The signature domain of the IMM family is the peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, which is in turn the drug binding domain. IMMs are classified by their ability to bind immunosuppressant drugs – CyPs (cyclophilins) bind cyclosporine A (CsA), and FKBPs (FK506-binding pro-teins) bind FK506 (Pratt and Toft 1997; Kang et al. 2008). In addition to the PPIase domain, there are three additional domains – the nucleotide-binding domain, (also called FKBD2 in FKBP proteins) where ATP binds, the calmodulin-binding domain, a poorly characterized domain able to interact with calmodulin, and tetratricopeptide repeat (TPR) domains, sequences of 34 amino acids repeated in tandem through which FKBPs bind to the HSP90 C-terminal sequence MEEVD (Davies et al. 2005; Wu et al. 2004). Mass spectrometry analysis showed that FKBP51 (FKBP5) and FKBP52 (FKBP4) form analogous complexes with GR:HSP90:STIP1:HSP70:ATP (Ebong IO et al. 2016). Binding of FKBP51 (FKBP5) and other immunophilins may weaken the association of TPR domain containing protein STIP1 with HSP90 complex (Li et al. 2011). |
| (summation) | [Reaction:5618105] FKBP5 binds HSP90:ATP:STIP1:HSP70:nascent protein [Homo sapiens] |
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