Structural highlights
Function
FKBP3_MOUSE FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins (By similarity).
Publication Abstract from PubMed
FKBP25 is a member of the super-family of peptidylprolyl cis/trans isomerases, which is a high affinity binder for the immunosuppressive antibiotic rapamycin (Rpm). FKBP25 isolated from natural sources, its recombinant murine homologue (mFKBP25) and their complexes with rapamycin bind to diverse DNAs, RNAs and heparin affinity beads. The recombinant mFKBP25/rapamycin complex binds to several proteins including the calcineurin-A/calcineurin-B/calmodulin complex and to elongation factor 1beta. We solved the X-ray structure of the C-terminal domain of mFKBP25 bound to rapamycin that has a higher resolution than of its human counterpart, and which clearly illustrates that the positively charged 40s loop is an epitope of the FK506-like binding domain (FKBD) for interactions with various biopolymers.
Diversified targets of FKBP25 and its complex with rapamycin.,Galat A, Thai R, Stura EA Int J Biol Macromol. 2014 May 29;69C:344-352. doi:, 10.1016/j.ijbiomac.2014.05.060. PMID:24879919[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Galat A, Thai R, Stura EA. Diversified targets of FKBP25 and its complex with rapamycin. Int J Biol Macromol. 2014 May 29;69C:344-352. doi:, 10.1016/j.ijbiomac.2014.05.060. PMID:24879919 doi:http://dx.doi.org/10.1016/j.ijbiomac.2014.05.060
