3KZ7
C-terminal domain of Murine FKBP25 rapamycin complex
Summary for 3KZ7
| Entry DOI | 10.2210/pdb3kz7/pdb |
| Related | 1PBK |
| Descriptor | FK506-binding protein 3, RAPAMYCIN IMMUNOSUPPRESSANT DRUG (3 entities in total) |
| Functional Keywords | fkpb ppiase rapamycin, isomerase, nucleus, phosphoprotein, rotamase, isomerase-inhibitor complex, isomerase/inhibitor |
| Biological source | Mus musculus (mouse) |
| Cellular location | Nucleus (By similarity): Q62446 |
| Total number of polymer chains | 1 |
| Total formula weight | 14198.51 |
| Authors | Stura, E.A.,Galat, A. (deposition date: 2009-12-08, release date: 2010-12-15, Last modification date: 2023-11-01) |
| Primary citation | Galat, A.,Thai, R.,Stura, E.A. Diversified targets of FKBP25 and its complex with rapamycin. Int.J.Biol.Macromol., 69:344-352, 2014 Cited by PubMed Abstract: 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 1β. 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. PubMed: 24879919DOI: 10.1016/j.ijbiomac.2014.05.060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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