- Peptidylprolyl isomerase A
-
Peptidylprolyl isomerase A also known as cyclophilin A or rotamase A is an enzyme that in humans is encoded by the PPIA gene.[1][2][3]
Contents
Function
This gene encodes 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 accelerates the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.[1]
Interactions
Peptidylprolyl isomerase A has been shown to interact with ITK.[4]
See also
References
- ^ a b "Entrez Gene: PPIA peptidylprolyl isomerase A (cyclophilin A)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5478.
- ^ Haendler B, Hofer E (July 1990). "Characterization of the human cyclophilin gene and of related processed pseudogenes". Eur. J. Biochem. 190 (3): 477–82. doi:10.1111/j.1432-1033.1990.tb15598.x. PMID 2197089.
- ^ Holzman TF, Egan DA, Edalji R, Simmer RL, Helfrich R, Taylor A, Burres NS (February 1991). "Preliminary characterization of a cloned neutral isoelectric form of the human peptidyl prolyl isomerase cyclophilin". J. Biol. Chem. 266 (4): 2474–9. PMID 1989998.
- ^ Brazin, Kristine N; Mallis Robert J, Fulton D Bruce, Andreotti Amy H (Feb. 2002). "Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (4): 1899–904. doi:10.1073/pnas.042529199. ISSN 0027-8424. PMC 122291. PMID 11830645. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=122291.
Further reading
- Franke EK, Luban J (1995). "Cyclophilin and gag in HIV-1 replication and pathogenesis". Adv. Exp. Med. Biol.. Advances in Experimental Medicine and Biology 374: 217–28. doi:10.1007/978-1-4615-1995-9_19. ISBN 978-0-306-45063-1. PMID 7572395.
- Sokolskaja E, Luban J (2006). "Cyclophilin, TRIM5, and innate immunity to HIV-1". Curr. Opin. Microbiol. 9 (4): 404–8. doi:10.1016/j.mib.2006.06.011. PMID 16815734.
PDB gallery 1ak4: HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID1awq: CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)1awr: CYPA COMPLEXED WITH HAGPIA1aws: SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)1awt: SECYPA COMPLEXED WITH HAGPIA1awu: CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC MONOMER)1awv: CYPA COMPLEXED WITH HVGPIA1bck: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-THR CYCLOSPORIN1cwa: X-RAY STRUCTURE OF A MONOMERIC CYCLOPHILIN A-CYCLOSPORIN A CRYSTAL COMPLEX AT 2.1 ANGSTROMS RESOLUTION1cwb: THE X-RAY STRUCTURE OF (MEBM2T)1-CYCLOSPORIN COMPLEXED WITH CYCLOPHILIN A PROVIDES AN EXPLANATION FOR ITS ANOMALOUSLY HIGH IMMUNOSUPPRESSIVE ACTIVITY1cwc: IMPROVED BINDING AFFINITY FOR CYCLOPHILIN A BY A CYCLOSPORIN DERIVATIVE SINGLY MODIFIED AT ITS EFFECTOR DOMAIN1cwf: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL CYCLOSPORIN1cwh: HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER CYCLOSPORIN1cwi: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-(N-METHYL)-D-ALANINE CYCLOSPORIN1cwj: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-S-METHYL-SARCOSINE CYCLOSPORIN1cwk: HUMAN CYCLOPHILIN A COMPLEXED WITH 1-(6,7-DIHYDRO)MEBMT 2-VAL 3-D-(2-S-METHYL)SARCOSINE CYCLOSPORIN1cwl: HUMAN CYCLOPHILIN A COMPLEXED WITH 4 4-HYDROXY-MELEU CYCLOSPORIN1cwm: HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORIN1cwo: HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN1fgl: Cyclophilin A complexed with a fragment of HIV-1 GAG protein1m63: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes1m9c: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.1m9d: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) O-type chimera Complex.1m9e: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A Complex.1m9f: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,A88M Complex.1m9x: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,A88M,G89A Complex.1m9y: X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,G89A Complex.1mf8: Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin1mik: THE ROLE OF WATER MOLECULES IN THE STRUCTURE-BASED DESIGN OF (5-HYDROXYNORVALINE)-2-CYCLOSPORIN: SYNTHESIS, BIOLOGICAL ACTIVITY, AND CRYSTALLOGRAPHIC ANALYSIS WITH CYCLOPHILIN A1nmk: The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-ray Crystal Structure and Binding Data1oca: HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES1rmh: RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL1vbs: STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE1vbt: Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF1w8l: ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES1w8m: ENZYMATIC AND STRUCTURAL CHARACTERISATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES1w8v: ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES1ynd: Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6A resolution1zkf: Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA2alf: crystal structure of human CypA mutant K131A2cpl: SIMILARITIES AND DIFFERENCES BETWEEN HUMAN CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS RESOLUTION2cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO2rma: Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A2rmb: Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A3cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO3cys: DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX4cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE HIS-PRO5cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PROThis protein-related article is a stub. You can help Wikipedia by expanding it.