4BFP
Crystal structure of human tankyrase 2 in complex with WIKI4
Summary for 4BFP
| Entry DOI | 10.2210/pdb4bfp/pdb |
| Descriptor | TANKYRASE-2, 2-[3-[[4-(4-methoxyphenyl)-5-pyridin-4-yl-1,2,4-triazol-3-yl]sulfanyl]propyl]benzo[de]isoquinoline-1,3-dione, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | transferase, protein-ligand complex, diphtheria toxin like fold, adp-ribosylation, transferase-transferase inhibitor complex |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 56157.78 |
| Authors | Haikarainen, T.,Narwal, M.,Lehtio, L. (deposition date: 2013-03-21, release date: 2013-06-19, Last modification date: 2024-05-08) |
| Primary citation | Haikarainen, T.,Venkannagari, H.,Narwal, M.,Obaji, E.,Lee, H.,Nkizinkiko, Y.,Lehtio, L. Structural Basis and Selectivity of Tankyrase Inhibition by a Wnt Signaling Inhibitor Wiki4 Plos One, 8:65404-, 2013 Cited by PubMed Abstract: Recently a novel inhibitor of Wnt signaling was discovered. The compound, WIKI4, was found to act through tankyrase inhibition and regulate β-catenin levels in many cancer cell lines and human embryonic stem cells. Here we confirm that WIKI4 is a high potency tankyrase inhibitor and that it selectively inhibits tankyrases over other ARTD enzymes tested. The binding mode of the compound to tankyrase 2 was determined by protein X-ray crystallography to 2.4 Å resolution. The structure revealed a novel binding mode to the adenosine subsite of the donor NAD(+) binding groove of the catalytic domain. Our results form a structural basis for further development of potent and selective tankyrase inhibitors based on the WIKI4 scaffold. PubMed: 23762361DOI: 10.1371/JOURNAL.PONE.0065404 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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