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FKBP3

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FKBP3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFKBP3, FKBP-25, FKBP-3, FKBP25, PPIase, FK506 binding protein 3, FKBP prolyl isomerase 3
External IDsOMIM: 186947; MGI: 1353460; HomoloGene: 1525; GeneCards: FKBP3; OMA:FKBP3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002013

NM_013902

RefSeq (protein)

NP_002004

NP_038930

Location (UCSC)Chr 14: 45.12 – 45.14 MbChr 12: 65.11 – 65.12 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

FK506-binding protein 3 also known as FKBP25 is a protein that in humans is encoded by the FKBP3 gene.[5][6][7]

Function

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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.[8][7]

Interactions

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FKBP3 has been shown to interact with YY1,[9] HDAC1,[9] Histone deacetylase 2,[9] DNA,[10] and Mdm2.[11] 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.[8][12]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100442Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020949Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hung DT, Schreiber SL (Jun 1992). "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein". Biochem. Biophys. Res. Commun. 184 (2): 733–8. doi:10.1016/0006-291X(92)90651-Z. PMID 1374240.
  6. ^ Porat R, Poutsiaka DD, Miller LC, Granowitz EV, Dinarello CA (May 1992). "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. doi:10.1096/fasebj.6.7.1532945. PMID 1532945. S2CID 29899093.
  7. ^ a b "Entrez Gene: FKBP3 FK506 binding protein 3, 25kDa".
  8. ^ a b Prakash A, Rajan S, Yoon HS (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. PMC 4941220. PMID 26749369.
  9. ^ a b c Yang WM, Yao YL, Seto E (Sep 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". EMBO J. 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. PMC 125595. PMID 11532945.
  10. ^ Prakash A, Shin J, Rajan S, Yoon HS (2016). "Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin". Nucleic Acids Res. 44 (6): 2909–25. doi:10.1093/nar/gkw001. PMC 4824100. PMID 26762975.
  11. ^ Ochocka AM, Kampanis P, Nicol S, Allende-Vega N, Cox M, Marcar L, Milne D, Fuller-Pace F, Meek D (Feb 2009). "FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53". FEBS Lett. 583 (4): 621–6. doi:10.1016/j.febslet.2009.01.009. PMID 19166840. S2CID 6110.
  12. ^ Prakash A, Shin J, Rajan S, Yoon HS (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. PMC 4824100. PMID 26762975.

Further reading

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  • 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