Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506
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...
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Published in | Protein science Vol. 25; no. 4; pp. 905 - 910 |
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Abstract | 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 Å 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.
Interactive Figure 1 | PDB Code(s): 5D75 |
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AbstractList | 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 Å 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.
Interactive Figure 1
| PDB Code(s):
5D75 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 Å 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. Interactive Figure 1 | PDB Code(s): 5D75 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 Å 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. 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 Å 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. Interactive Figure 1 | PDB Code(s): 5D75 |
Author | Yoon, Ho Sup Prakash, Ajit Rajan, Sreekanth |
AuthorAffiliation | 1 School of Biological Sciences Nanyang Technological University 60 Nanyang Drive Singapore 637551 Singapore 2 Department of Genetic Engineering College of Life Sciences, Kyung Hee University Yongin‐si Gyeonggi‐do 446‐701 Republic of Korea |
AuthorAffiliation_xml | – name: 2 Department of Genetic Engineering College of Life Sciences, Kyung Hee University Yongin‐si Gyeonggi‐do 446‐701 Republic of Korea – name: 1 School of Biological Sciences Nanyang Technological University 60 Nanyang Drive Singapore 637551 Singapore |
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SubjectTerms | Affinity Binding Binding Sites Crystal structure Crystallography, X-Ray Drug interaction FK506 FKBD25 FKBP FKBP25 Humans immunophilin Immunosuppressive agents inhibitor Microheterogeneity Models, Molecular Protein Binding Protein Conformation Protein Structure Report Protein Structure Reports Proteins Rapamycin Sirolimus - metabolism Substrate Specificity Tacrolimus Tacrolimus - metabolism Tacrolimus Binding Proteins - chemistry Tacrolimus Binding Proteins - metabolism |
Title | Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506 |
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