4f1q
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F1Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[4f1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F1Q FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0RZ:(2E)-4-[(3-CARBAMOYLPHENYL)AMINO]-4-OXOBUT-2-ENOIC+ACID'>0RZ</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0RZ:(2E)-4-[(3-CARBAMOYLPHENYL)AMINO]-4-OXOBUT-2-ENOIC+ACID'>0RZ</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1q OCA], [https://pdbe.org/4f1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f1q RCSB], [https://www.ebi.ac.uk/pdbsum/4f1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f1q ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1q OCA], [https://pdbe.org/4f1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f1q RCSB], [https://www.ebi.ac.uk/pdbsum/4f1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f1q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PAR14_HUMAN PAR14_HUMAN] Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. | [https://www.uniprot.org/uniprot/PAR14_HUMAN PAR14_HUMAN] Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The diphtheria toxin-like ADP-ribosyltransferases (ARTDs) are an enzyme family that catalyzes the transfer of ADP-ribose units onto substrate proteins by using nicotinamide adenine dinucleotide (NAD(+)) as a cosubstrate. They have a documented role in chromatin remodelling and DNA repair, and inhibitors of ARTD1 and 2 (PARP1 and 2) are currently in clinical trials for the treatment of cancer. The detailed function of most other ARTDs is still unknown. By using virtual screening, we identified small ligands of ARTD7 (PARP15/BAL3) and ARTD8 (PARP14/BAL2). Thermal-shift assays confirmed that 16 compounds, belonging to eight structural classes, bound to ARTD7/ARTD8. Affinity measurements with isothermal titration calorimetry for two isomers of the most promising hit compound confirmed binding in the low micromolar range to ARTD8. Crystal structures showed anchoring of the hits in the nicotinamide pocket. These results form a starting point in the development of chemical tools for the study of the role and function of ARTD7 and ARTD8. | ||
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| - | Discovery of Ligands for ADP-Ribosyltransferases via Docking-Based Virtual Screening.,Andersson CD, Karlberg T, Ekblad T, Lindgren AE, Thorsell AG, Spjut S, Uciechowska U, Niemiec MS, Wittung-Stafshede P, Weigelt J, Elofsson M, Schuler H, Linusson A J Med Chem. 2012 Aug 20. PMID:22823910<ref>PMID:22823910</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4f1q" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | *[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 15:13, 14 March 2024
Human Artd8 (Parp14, Bal2) - catalytic domain in complex with A16(E)
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Categories: Homo sapiens | Large Structures | Andersson CD | Ekblad T | Elofsson M | Karlberg T | Lindgren A | Linusson A | Schuler H | Spjut S | Thorsell AG | Weigelt J
