4gv7
From Proteopedia
Line 1: | Line 1: | ||
- | + | {{STRUCTURE_4gv7| PDB=4gv7 | SCENE= }} | |
+ | ===Human ARTD1 (PARP1) - Catalytic domain in complex with inhibitor ME0328=== | ||
+ | {{ABSTRACT_PUBMED_23742272}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/PARP1_HUMAN PARP1_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.<ref>PMID:17177976</ref> <ref>PMID:18172500</ref> <ref>PMID:19344625</ref> <ref>PMID:19661379</ref> | ||
- | + | ==About this Structure== | |
+ | [[4gv7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GV7 OCA]. | ||
- | + | ==Reference== | |
+ | <ref group="xtra">PMID:023742272</ref><references group="xtra"/><references/> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Andersson, C D.]] | ||
+ | [[Category: Ekblad, T.]] | ||
+ | [[Category: Elofsson, M.]] | ||
+ | [[Category: Karlberg, T.]] | ||
+ | [[Category: Lindgren, A E.G.]] | ||
+ | [[Category: Linusson, A.]] | ||
+ | [[Category: Schuler, H.]] | ||
+ | [[Category: Spjut, S.]] | ||
+ | [[Category: Thorsell, A G.]] | ||
+ | [[Category: Weigelt, J.]] | ||
+ | [[Category: Adp-ribose]] | ||
+ | [[Category: Adp-ribose transferase]] | ||
+ | [[Category: Adp-ribosylation]] | ||
+ | [[Category: Artd transferase domain]] | ||
+ | [[Category: Artd1]] | ||
+ | [[Category: Nad]] | ||
+ | [[Category: Parp1]] | ||
+ | [[Category: Transferase-transferase inhibitor complex]] |
Revision as of 16:10, 19 June 2013
Contents |
Human ARTD1 (PARP1) - Catalytic domain in complex with inhibitor ME0328
Template:ABSTRACT PUBMED 23742272
Function
[PARP1_HUMAN] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.[1] [2] [3] [4]
About this Structure
4gv7 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Lindgren AE, Karlberg T, Thorsell AG, Hesse M, Spjut S, Ekblad T, Andersson CD, Pinto AF, Weigelt J, Hottiger MO, Linusson A, Elofsson M, Schuler H. A PARP inhibitor with selectivity toward ADP-ribosyltransferase ARTD3/PARP3. ACS Chem Biol. 2013 Jun 6. PMID:23742272 doi:10.1021/cb4002014
- ↑ Maruyama T, Nara K, Yoshikawa H, Suzuki N. Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells. Clin Exp Immunol. 2007 Jan;147(1):164-75. PMID:17177976 doi:10.1111/j.1365-2249.2006.03249.x
- ↑ Ahel I, Ahel D, Matsusaka T, Clark AJ, Pines J, Boulton SJ, West SC. Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature. 2008 Jan 3;451(7174):81-5. doi: 10.1038/nature06420. PMID:18172500 doi:10.1038/nature06420
- ↑ Reinemund J, Seidel K, Steckelings UM, Zaade D, Klare S, Rompe F, Katerbaum M, Schacherl J, Li Y, Menk M, Schefe JH, Goldin-Lang P, Szabo C, Olah G, Unger T, Funke-Kaiser H. Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes. Biochem Pharmacol. 2009 Jun 15;77(12):1795-805. doi: 10.1016/j.bcp.2009.02.025., Epub 2009 Mar 19. PMID:19344625 doi:10.1016/j.bcp.2009.02.025
- ↑ Ahel D, Horejsi Z, Wiechens N, Polo SE, Garcia-Wilson E, Ahel I, Flynn H, Skehel M, West SC, Jackson SP, Owen-Hughes T, Boulton SJ. Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1. Science. 2009 Sep 4;325(5945):1240-3. doi: 10.1126/science.1177321. Epub 2009 Aug, 6. PMID:19661379 doi:10.1126/science.1177321
Categories: Homo sapiens | Andersson, C D. | Ekblad, T. | Elofsson, M. | Karlberg, T. | Lindgren, A E.G. | Linusson, A. | Schuler, H. | Spjut, S. | Thorsell, A G. | Weigelt, J. | Adp-ribose | Adp-ribose transferase | Adp-ribosylation | Artd transferase domain | Artd1 | Nad | Parp1 | Transferase-transferase inhibitor complex