| Glutathione S-transferase pi 1 |
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PDB rendering based on 10gs. |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB
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| List of PDB id codes |
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10GS, 11GS, 12GS, 13GS, 14GS, 16GS, 17GS, 18GS, 19GS, 1AQV, 1AQW, 1AQX, 1EOG, 1EOH, 1GSS, 1KBN, 1LBK, 1MD3, 1MD4, 1PGT, 1PX6, 1PX7, 1ZGN, 20GS, 22GS, 2A2R, 2A2S, 2GSS, 2J9H, 2PGT, 3CSH, 3CSI, 3CSJ, 3DD3, 3DGQ, 3GSS, 3GUS, 3HJM, 3HJO, 3HKR, 3IE3, 3KM6, 3KMN, 3KMO, 3N9J, 3PGT, 4GSS, 4PGT, 5GSS, 6GSS, 7GSS, 8GSS, 9GSS
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| Identifiers |
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| Symbols | GSTP1; DFN7; FAEES3; GST3; GSTP; PI |
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| External IDs | OMIM: 134660 MGI: 95864 HomoloGene: 660 ChEMBL: 3902 GeneCards: GSTP1 Gene |
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| EC number | 2.5.1.18 |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
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| Species | Human | Mouse | |
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| Entrez | 2950 | 14869 | |
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| Ensembl | ENSG00000084207 | ENSMUSG00000038155 | |
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| UniProt | P09211 | P46425 | |
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| RefSeq (mRNA) | NM_000852 | NM_181796 | |
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| RefSeq (protein) | NP_000843 | NP_861461 | |
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| Location (UCSC) | Chr 11:
67.35 – 67.35 Mb | Chr 19:
4.04 – 4.04 Mb | |
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| PubMed search | | | |
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Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.[1][2]
Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into 4 main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.[3]
Interactions
GSTP1 has been shown to interact with Fanconi anemia, complementation group C[4][5] and MAPK8.[6]
References
- ↑ Bora PS, Bora NS, Wu XL, Lange LG (Oct 1991). "Molecular cloning, sequencing, and expression of human myocardial fatty acid ethyl ester synthase-III cDNA". J Biol Chem 266 (25): 16774–7. PMID 1885604.
- ↑ Smith CM, Bora PS, Bora NS, Jones C, Gerhard DS (Nov 1995). "Genetic and radiation-reduced somatic cell hybrid sublocalization of the human GSTP1 gene". Cytogenet Cell Genet 71 (3): 235–9. doi:10.1159/000134117. PMID 7587384.
- ↑ "Entrez Gene: GSTP1 glutathione S-transferase pi".
- ↑ Cumming, R C; Lightfoot J, Beard K, Youssoufian H, O'Brien P J, Buchwald M (Jul 2001). "Fanconi anemia group C protein prevents apoptosis in hematopoietic cells through redox regulation of GSTP1". Nat. Med. (United States) 7 (7): 814–20. doi:10.1038/89937. ISSN 1078-8956. PMID 11433346.
- ↑ Reuter, Tanja Y; Medhurst Annette L, Waisfisz Quinten, Zhi Yu, Herterich Sabine, Hoehn Holger, Gross Hans J, Joenje Hans, Hoatlin Maureen E, Mathew Christopher G, Huber Pia A J (Oct 2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. (United States) 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. ISSN 0014-4827. PMID 14499622.
- ↑ Wang, T; Arifoglu P, Ronai Z, Tew K D (Jun 2001). "Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus". J. Biol. Chem. (United States) 276 (24): 20999–1003. doi:10.1074/jbc.M101355200. ISSN 0021-9258. PMID 11279197.
Further reading
- Strange RC, Fryer AA (1999). "The glutathione S-transferases: influence of polymorphism on cancer susceptibility.". IARC Sci. Publ. (148): 231–49. PMID 10493261.
- Kellen E, Hemelt M, Broberg K et al. (2007). "Pooled analysis and meta-analysis of the glutathione S-transferase P1 Ile 105Val polymorphism and bladder cancer: a HuGE-GSEC review". Am. J. Epidemiol. 165 (11): 1221–30. doi:10.1093/aje/kwm003. PMID 17404387.
- Sekine I, Minna JD, Nishio K et al. (2007). "A literature review of molecular markers predictive of clinical response to cytotoxic chemotherapy in patients with lung cancer". Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer 1 (1): 31–7. PMID 17409824.
PDB gallery |
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| 10gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117 |
| 11gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE (FORM II) |
| 12gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE |
| 13gs: GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE |
| 14gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1 |
| 16gs: GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3 |
| 17gs: GLUTATHIONE S-TRANSFERASE P1-1 |
| 18gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE |
| 19gs: GLUTATHIONE S-TRANSFERASE P1-1 |
| 1aqv: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE |
| 1aqw: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH GLUTATHIONE |
| 1aqx: GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX |
| 1eog: CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE |
| 1eoh: GLUTATHIONE TRANSFERASE P1-1 |
| 1gss: THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION |
| 1kbn: Glutathione transferase mutant |
| 1lbk: Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme |
| 1md3: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to alanine |
| 1md4: A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine |
| 1pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE |
| 1px6: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine |
| 1px7: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate |
| 1zgn: Crystal Structure of the Glutathione Transferase Pi in Complex with Dinitrosyl-diglutathionyl Iron Complex |
| 20gs: GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE |
| 22gs: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y49F MUTANT |
| 2a2r: Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione |
| 2a2s: Crystal Structure of Human Glutathione Transferase in complex with S-nitrosoglutathione in the absence of reducing agent |
| 2gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID |
| 2j9h: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE-S-TRANSFERASE P1-1 CYS-FREE MUTANT IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.4 A RESOLUTION |
| 2pgt: CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE |
| 3gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 IN COMPLEX WITH ETHACRYNIC ACID-GLUTATHIONE CONJUGATE |
| 3pgt: CRYSTAL STRUCTURE OF HGSTP1-1[I104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE |
| 4gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1 Y108F MUTANT |
| 4pgt: CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE |
| 5gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE |
| 6gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE |
| 7gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE |
| 8gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH GLUTATHIONE |
| 9gss: HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH S-HEXYL GLUTATHIONE |
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