| Peptidylprolyl isomerase A (cyclophilin A) |
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PDB rendering based on 1ak4. |
| Available structures |
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Ortholog search: PDBe, RCSB
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| List of PDB id codes |
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1AK4, 1AWQ, 1AWR, 1AWS, 1AWT, 1AWU, 1AWV, 1BCK, 1CWA, 1CWB, 1CWC, 1CWF, 1CWH, 1CWI, 1CWJ, 1CWK, 1CWL, 1CWM, 1CWO, 1FGL, 1M63, 1M9C, 1M9D, 1M9E, 1M9F, 1M9X, 1M9Y, 1MF8, 1MIK, 1NMK, 1OCA, 1RMH, 1VBS, 1VBT, 1W8L, 1W8M, 1W8V, 1YND, 1ZKF, 2ALF, 2CPL, 2CYH, 2RMA, 2RMB, 2X25, 2X2A, 2X2C, 2X2D, 2XGY, 3CYH, 3CYS, 3K0M, 3K0N, 3K0O, 3K0P, 3K0Q, 3K0R, 3ODI, 3ODL, 3RDD, 4CYH, 4IPZ, 5CYH
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| Identifiers |
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| Symbols | PPIA; CYPA; CYPH |
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| External IDs | OMIM: 123840 MGI: 3648545 HomoloGene: 115610 ChEMBL: 1949 GeneCards: PPIA Gene |
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| EC number | 5.2.1.8 |
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| Orthologs |
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| Species | Human | Mouse | |
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| Entrez | 5478 | 268373 | |
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| Ensembl | ENSG00000196262 | ENSMUSG00000062933 | |
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| UniProt | P62937 | P17742 | |
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| RefSeq (mRNA) | NM_021130 | NM_008907 | |
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| RefSeq (protein) | NP_066953 | NP_032933 | |
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| Location (UCSC) | Chr 7:
44.84 – 44.86 Mb | Chr 11:
6.42 – 6.42 Mb | |
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| PubMed search | | | |
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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]
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
- ↑ 1.0 1.1 "Entrez Gene: PPIA peptidylprolyl isomerase A (cyclophilin A)".
- ↑ 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.
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 |
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| 1ak4: HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID |
| 1awq: CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER) |
| 1awr: CYPA COMPLEXED WITH HAGPIA |
| 1aws: SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER) |
| 1awt: SECYPA COMPLEXED WITH HAGPIA |
| 1awu: CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC MONOMER) |
| 1awv: CYPA COMPLEXED WITH HVGPIA |
| 1bck: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-THR CYCLOSPORIN |
| 1cwa: X-RAY STRUCTURE OF A MONOMERIC CYCLOPHILIN A-CYCLOSPORIN A CRYSTAL COMPLEX AT 2.1 ANGSTROMS RESOLUTION |
| 1cwb: THE X-RAY STRUCTURE OF (MEBM2T)1-CYCLOSPORIN COMPLEXED WITH CYCLOPHILIN A PROVIDES AN EXPLANATION FOR ITS ANOMALOUSLY HIGH IMMUNOSUPPRESSIVE ACTIVITY |
| 1cwc: IMPROVED BINDING AFFINITY FOR CYCLOPHILIN A BY A CYCLOSPORIN DERIVATIVE SINGLY MODIFIED AT ITS EFFECTOR DOMAIN |
| 1cwf: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL CYCLOSPORIN |
| 1cwh: HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER CYCLOSPORIN |
| 1cwi: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-(N-METHYL)-D-ALANINE CYCLOSPORIN |
| 1cwj: HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3-S-METHYL-SARCOSINE CYCLOSPORIN |
| 1cwk: HUMAN CYCLOPHILIN A COMPLEXED WITH 1-(6,7-DIHYDRO)MEBMT 2-VAL 3-D-(2-S-METHYL)SARCOSINE CYCLOSPORIN |
| 1cwl: HUMAN CYCLOPHILIN A COMPLEXED WITH 4 4-HYDROXY-MELEU CYCLOSPORIN |
| 1cwm: HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORIN |
| 1cwo: HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN |
| 1fgl: Cyclophilin A complexed with a fragment of HIV-1 GAG protein |
| 1m63: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes |
| 1m9c: 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 cyclophilin |
| 1mik: THE ROLE OF WATER MOLECULES IN THE STRUCTURE-BASED DESIGN OF (5-HYDROXYNORVALINE)-2-CYCLOSPORIN: SYNTHESIS, BIOLOGICAL ACTIVITY, AND CRYSTALLOGRAPHIC ANALYSIS WITH CYCLOPHILIN A |
| 1nmk: The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-ray Crystal Structure and Binding Data |
| 1oca: HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES |
| 1rmh: RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL |
| 1vbs: STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)ALA CONTAINING TETRAPEPTIDE |
| 1vbt: Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF |
| 1w8l: ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES |
| 1w8m: ENZYMATIC AND STRUCTURAL CHARACTERISATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES |
| 1w8v: ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES |
| 1ynd: Structure of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A at 1.6A resolution |
| 1zkf: Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA |
| 2alf: crystal structure of human CypA mutant K131A |
| 2cpl: SIMILARITIES AND DIFFERENCES BETWEEN HUMAN CYCLOPHILIN A AND OTHER BETA-BARREL STRUCTURES. STRUCTURAL REFINEMENT AT 1.63 ANGSTROMS RESOLUTION |
| 2cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO |
| 2rma: Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A |
| 2rmb: Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A |
| 3cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO |
| 3cys: DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX |
| 4cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE HIS-PRO |
| 5cyh: CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO |
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