Biology:FKBP3
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
FK506-binding protein 3 also known as FKBP25 is a protein that in humans is encoded by the FKBP3 gene.[1][2][3]
Function
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It has a higher affinity for rapamycin than for FK506 and thus may be an important target molecule for immunosuppression by rapamycin.[4][3]
Interactions
FKBP3 has been shown to interact with YY1,[5] HDAC1,[5] Histone deacetylase 2,[5] DNA,[6] and Mdm2.[7] Both crystal structure of FKBP25 with FK506 and the NMR structure of full length FKBP25 has been published with PDB ID 5D75 and 2MPH respectively.[4][8]
References
- ↑ "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein". Biochem. Biophys. Res. Commun. 184 (2): 733–8. Jun 1992. doi:10.1016/0006-291X(92)90651-Z. PMID 1374240.
- ↑ "Interleukin-1 (IL-1) receptor blockade reduces endotoxin and Borrelia burgdorferi-stimulated IL-8 synthesis in human mononuclear cells". FASEB J. 6 (7): 2482–6. May 1992. doi:10.1096/fasebj.6.7.1532945. PMID 1532945.
- ↑ 3.0 3.1 "Entrez Gene: FKBP3 FK506 binding protein 3, 25kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2287.
- ↑ 4.0 4.1 Prakash, Ajit; Rajan, Sreekanth; Yoon, Ho Sup (April 2016). "Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506". Protein Science 25 (4): 905–910. doi:10.1002/pro.2875. ISSN 1469-896X. PMID 26749369.
- ↑ 5.0 5.1 5.2 "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". EMBO J. 20 (17): 4814–25. Sep 2001. doi:10.1093/emboj/20.17.4814. PMID 11532945.
- ↑ "Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin". Nucleic Acids Res. 44 (6): 2909–25. 2016. doi:10.1093/nar/gkw001. PMID 26762975.
- ↑ "FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53". FEBS Lett. 583 (4): 621–6. Feb 2009. doi:10.1016/j.febslet.2009.01.009. PMID 19166840.
- ↑ Prakash, Ajit; Shin, Joon; Rajan, Sreekanth; Yoon, Ho Sup (2016-04-07). "Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin". Nucleic Acids Research 44 (6): 2909–2925. doi:10.1093/nar/gkw001. ISSN 0305-1048. PMID 26762975. PMC 4824100. https://doi.org/10.1093/nar/gkw001.
Further reading
- "Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25". J. Biol. Chem. 267 (16): 10942–5. 1992. doi:10.1016/S0021-9258(19)49856-6. PMID 1375932.
- "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein". Biochem. Biophys. Res. Commun. 185 (1): 298–303. 1992. doi:10.1016/S0006-291X(05)80990-8. PMID 1376117.
- "The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin". Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7769–73. 1993. doi:10.1073/pnas.90.16.7769. PMID 7689229. Bibcode: 1993PNAS...90.7769J.
- "Purification of CpG islands using a methylated DNA binding column". Nat. Genet. 6 (3): 236–44. 1994. doi:10.1038/ng0394-236. PMID 8012384.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Cloning and identification of a novel cDNA which may be associated with FKBP25". Biochem. Genet. 40 (9–10): 303–10. 2002. doi:10.1023/A:1020256718720. PMID 12392168.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
External links
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Peptidyl-prolyl cis-trans isomerase FKBP3
- PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Peptidyl-prolyl cis-trans isomerase FKBP3
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