6ghk: Difference between revisions

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'''Unreleased structure'''


The entry 6ghk is ON HOLD
==Human PARP1 (ARTD1) - Catalytic domain in complex with inhibitor ME0527==
 
<StructureSection load='6ghk' size='340' side='right'caption='[[6ghk]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
Authors: Karlberg, T., Thorsell, A.G., Lindgren, A.E.G., Moche, M., Brock, J., Ekblad, T., Spjut, S., Elofsson, M., Schuler, H.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ghk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GHK FirstGlance]. <br>
Description: Human PARP1 (ARTD1) -Catalytic domain in complex with inhibitor ME0527
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EZ2:~{N}-[(1~{R})-1-(4-imidazol-1-ylphenyl)ethyl]-3-(4-oxidanylidene-1~{H}-quinazolin-2-yl)propanamide'>EZ2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>
[[Category: Lindgren, A.E.G]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ghk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ghk OCA], [http://pdbe.org/6ghk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ghk RCSB], [http://www.ebi.ac.uk/pdbsum/6ghk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ghk ProSAT]</span></td></tr>
</table>
== 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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Brock, J]]
[[Category: Ekblad, T]]
[[Category: Ekblad, T]]
[[Category: Thorsell, A.G]]
[[Category: Elofsson, M]]
[[Category: Spjut, S]]
[[Category: Karlberg, T]]
[[Category: Karlberg, T]]
[[Category: Elofsson, M]]
[[Category: Lindgren, A E.G]]
[[Category: Brock, J]]
[[Category: Moche, M]]
[[Category: Schuler, H]]
[[Category: Schuler, H]]
[[Category: Moche, M]]
[[Category: Spjut, S]]
[[Category: Thorsell, A G]]
[[Category: Adp-ribosyl transferase]]
[[Category: Inhibitor]]
[[Category: Protein-ligand complex]]
[[Category: Transferase]]

Latest revision as of 09:46, 23 May 2019

Human PARP1 (ARTD1) - Catalytic domain in complex with inhibitor ME0527Human PARP1 (ARTD1) - Catalytic domain in complex with inhibitor ME0527

Structural highlights

6ghk is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

6ghk, resolution 2.28Å

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