Structural highlights
Function
FKBP3_HUMAN 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.
Publication Abstract from PubMed
Human FKBP25 (hFKBP25) is a nuclear immunophilin and interacts with several nuclear proteins, hence involving in many nuclear events. Similar to other FKBPs, FK506 binding domain (FKBD) of hFKBP25 also binds to immunosuppressive drugs such as rapamycin and FK506, albeit with a lower affinity for the latter. The molecular basis underlying this difference in affinity could not be addressed due to the lack of the crystal structure of hFKBD25 in complex with FK506. Here, we report the crystal structure of hFKBD25 in complex with FK506 determined at 1.8 A resolution and its comparison with the hFKBD25-rapamycin complex, bringing out the microheterogeneity in the mode of interaction of these drugs, which could possibly explain the lower affinity for FK506.
Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.,Prakash A, Rajan S, Yoon HS Protein Sci. 2016 Apr;25(4):905-10. doi: 10.1002/pro.2875. Epub 2016 Feb 1. PMID:26749369[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Prakash A, Rajan S, Yoon HS. Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506. Protein Sci. 2016 Apr;25(4):905-10. doi: 10.1002/pro.2875. Epub 2016 Feb 1. PMID:26749369 doi:http://dx.doi.org/10.1002/pro.2875
