2VPP
Drosophila melanogaster deoxyribonucleoside kinase successfully activates gemcitabine in transduced cancer cell lines
Summary for 2VPP
| Entry DOI | 10.2210/pdb2vpp/pdb |
| Related | 1J90 1OE0 1OT3 1ZM7 1ZMX 2JCS 2VP0 2VP2 2VP4 2VP5 2VP6 2VP9 |
| Descriptor | DEOXYNUCLEOSIDE KINASE, GEMCITABINE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | kinase, cancer, transferase, atp-binding, phosphoprotein, nucleoside analogs, nucleotide-binding, structure-function relationship, gemcitabine, gene therapy, dna synthesis |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 2 |
| Total formula weight | 54531.94 |
| Authors | Knecht, W.,Mikkelsen, N.E.,Clausen, A.,Willer, M.,Gojkovic, Z.,Piskur, J. (deposition date: 2008-03-03, release date: 2009-03-24, Last modification date: 2023-12-13) |
| Primary citation | Knecht, W.,Mikkelsen, N.E.,Clausen, A.,Willer, M.,Eklund, H.,Gojkovic, Z.,Piskur, J. Drosophila Melanogaster Deoxyribonucleoside Kinase Activates Gemcitabine. Biochem.Biophys.Res.Commun., 382:430-, 2009 Cited by PubMed Abstract: Drosophila melanogaster multisubstrate deoxyribonucleoside kinase (Dm-dNK) can additionally sensitize human cancer cell lines towards the anti-cancer drug gemcitabine. We show that this property is based on the Dm-dNK ability to efficiently phosphorylate gemcitabine. The 2.2A resolution structure of Dm-dNK in complex with gemcitabine shows that the residues Tyr70 and Arg105 play a crucial role in the firm positioning of gemcitabine by extra interactions made by the fluoride atoms. This explains why gemcitabine is a good substrate for Dm-dNK. PubMed: 19285960DOI: 10.1016/J.BBRC.2009.03.041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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