3KR7
Human tankyrase 2 - catalytic PARP domain
Summary for 3KR7
| Entry DOI | 10.2210/pdb3kr7/pdb |
| Related | 3KR8 |
| Descriptor | Tankyrase-2, ZINC ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | catalytic fragment, parp, structural genomics, structural genomics consortium, sgc, adp-ribosylation, ank repeat, chromosomal protein, glycosyltransferase, golgi apparatus, membrane, mrna transport, nad, nuclear pore complex, nucleus, phosphorylation, protein transport, telomere, transferase, translocation, transport, wnt-signalling |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q9H2K2 |
| Total number of polymer chains | 1 |
| Total formula weight | 27741.49 |
| Authors | Karlberg, T.,Schutz, P.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kallas, A.,Kotenyova, T.,Kotzsch, A.,Kraulis, P.,Nielsen, T.K.,Moche, M.,Nordlund, P.,Nyman, T.,Persson, C.,Siponen, M.I.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Weigelt, J.,Welin, M.,Wisniewska, M.,Schuler, H.,Structural Genomics Consortium (SGC) (deposition date: 2009-11-18, release date: 2009-12-15, Last modification date: 2023-11-01) |
| Primary citation | Karlberg, T.,Markova, N.,Johansson, I.,Hammarstrom, M.,Schutz, P.,Weigelt, J.,Schuler, H. Structural basis for the interaction between tankyrase-2 and a potent Wnt-signaling inhibitor. J.Med.Chem., 53:5352-5355, 2010 Cited by PubMed Abstract: We report two crystal structures of the PARP domain of human tankyrase-2 (TNKS2). Tankyrases are involved in fundamental cellular processes such as telomere homeostasis and Wnt signaling. The complex of TNKS2 with the potent inhibitor XAV939 provides insights into the molecular basis of the strong interaction and suggests routes for further development of tankyrase inhibitors. PubMed: 20565110DOI: 10.1021/jm100249w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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