PPID
Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene.[1]
Function
The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant ciclosporin.[1]
References
Further reading
- Berardini TZ, Bollman K, Sun H, Poethig RS (2001). "Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40.". Science 291 (5512): 2405–7. doi:10.1126/science.1057144. PMID 11264535.
- Kieffer LJ, Thalhammer T, Handschumacher RE (1992). "Isolation and characterization of a 40-kDa cyclophilin-related protein.". J. Biol. Chem. 267 (8): 5503–7. PMID 1544925.
- Hoffmann K, Kakalis LT, Anderson KS, et al. (1995). "Expression of human cyclophilin-40 and the effect of the His141-->Trp mutation on catalysis and ciclosporin A binding.". Eur. J. Biochem. 229 (1): 188–93. doi:10.1111/j.1432-1033.1995.tb20454.x. PMID 7744028.
- Kieffer LJ, Seng TW, Li W, et al. (1993). "Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization.". J. Biol. Chem. 268 (17): 12303–10. PMID 8509368.
- Yokoi H, Shimizu Y, Anazawa H, et al. (1996). "The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene.". Genomics 35 (3): 448–55. doi:10.1006/geno.1996.0384. PMID 8812478.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Silverstein AM, Galigniana MD, Chen MS, et al. (1997). "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.". J. Biol. Chem. 272 (26): 16224–30. doi:10.1074/jbc.272.26.16224. PMID 9195923.
- Young JC, Obermann WM, Hartl FU (1998). "Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90.". J. Biol. Chem. 273 (29): 18007–10. doi:10.1074/jbc.273.29.18007. PMID 9660753.
- Mark PJ, Ward BK, Kumar P, et al. (2001). "Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock.". Cell Stress Chaperones 6 (1): 59–70. doi:10.1379/1466-1268(2001)006<0059:HCIAHS>2.0.CO;2. PMC 434384. PMID 11525244. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=434384.
- Ward BK, Allan RK, Mok D, et al. (2002). "A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90.". J. Biol. Chem. 277 (43): 40799–809. doi:10.1074/jbc.M207097200. PMID 12145316.
- McStay GP, Clarke SJ, Halestrap AP (2002). "Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore.". Biochem. J. 367 (Pt 2): 541–8. doi:10.1042/BJ20011672. PMC 1222909. PMID 12149099. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222909.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- Schubert A, Grimm S (2004). "Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor.". Cancer Res. 64 (1): 85–93. doi:10.1158/0008-5472.CAN-03-0476. PMID 14729611.
- Machida K, Osada H (2004). "Molecular interaction between cyclophilin D and adenine nucleotide translocase in cytochrome c release: does it determine whether cytochrome c release is dependent on permeability transition or not?". Ann. N. Y. Acad. Sci. 1010: 182–5. doi:10.1196/annals.1299.031. PMID 15033717.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Carrello A, Allan RK, Morgan SL, et al. (2005). "Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.". Cell Stress Chaperones 9 (2): 167–81. doi:10.1379/CSC-26R.1. PMC 1065296. PMID 15497503. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1065296.
- Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells.". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
- Machida K, Ohta Y, Osada H (2006). "Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells.". J. Biol. Chem. 281 (20): 14314–20. doi:10.1074/jbc.M513297200. PMID 16551620.
- Mok D, Allan RK, Carrello A, et al. (2006). "The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.". FEBS Lett. 580 (11): 2761–8. doi:10.1016/j.febslet.2006.04.039. PMID 16650407.
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PDB gallery
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1ihg: Bovine Cyclophilin 40, monoclinic form
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1iip: Bovine Cyclophilin 40, Tetragonal Form
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