2WPU
Chaperoned ruthenium metallodrugs that recognize telomeric DNA
Summary for 2WPU
| Entry DOI | 10.2210/pdb2wpu/pdb |
| Related | 1DF8 1HQQ 1HXL 1HXZ 1HY2 1I9H 1KFF 1KL3 1KL4 1KL5 1LCV 1LCW 1LCZ 1LUQ 1MEP 1MK5 1MM9 1MOY 1N43 1N4J 1N7Y 1N9M 1N9Y 1NBX 1NC9 1NDJ 1NQM 1PTS 1RST 1RSU 1RXH 1RXJ 1RXK 1SLD 1SLE 1SLF 1SLG 1SRE 1SRF 1SRG 1SRH 1SRI 1SRJ 1STP 1STR 1STS 1SWA 1SWB 1SWC 1SWD 1SWE 1SWF 1SWG 1SWH 1SWJ 1SWK 1SWL 1SWN 1SWO 1SWP 1SWQ 1SWR 1SWS 1SWT 1SWU 1VWA 1VWB 1VWC 1VWD 1VWE 1VWF 1VWG 1VWH 1VWI 1VWJ 1VWK 1VWL 1VWM 1VWN 1VWO 1VWP 1VWQ 1VWR 2BC3 2F01 2IZA 2IZB 2IZC 2IZD 2IZE 2IZF 2IZG 2IZH 2IZI 2IZJ 2IZK 2IZL 2RTA 2RTB 2RTC 2RTD 2RTE 2RTF 2RTG 2RTH 2RTI 2RTJ 2RTK 2RTL 2RTM 2RTN 2RTO 2RTP 2RTQ 2RTR |
| Descriptor | STREPTAVIDIN, (3AS,4S,6AR)-4-(5-((3R,4R)-3,4-DIAMINOPYRROLIDIN-1-YL)-5-OXOPENTYL)TETRAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-2(3H)-ONE-P-CYMENE-CHLORO-RUTHENIUM(III), SULFATE ION, ... (5 entities in total) |
| Functional Keywords | biotin binding protein |
| Biological source | STREPTOMYCES AVIDINII |
| Total number of polymer chains | 1 |
| Total formula weight | 17356.36 |
| Authors | Heinisch, T.,Schirmer, T.,Zimbron, J.M.,Sardo, A.,Wohlschlager, T.,Gradinaru, J.,Creus, M.,Ward, T.R. (deposition date: 2009-08-10, release date: 2010-10-13, Last modification date: 2023-12-20) |
| Primary citation | Zimbron, J.M.,Sardo, A.,Heinisch, T.,Wohlschlager, T.,Gradinaru, J.,Massa, C.,Schirmer, T.,Creus, M.,Ward, T.R. Chemo-Genetic Optimization of DNA Recognition by Metallodrugs Using a Presenter-Protein Strategy. Chemistry, 16:12883-, 2010 Cited by PubMed Abstract: The mode of action of precious metal anticancer metallodrugs is generally believed to involve DNA as a target. However, the poor specificity of such drugs often requires high doses and leads to undesirable side-effects. With the aim of improving the specificity of a ruthenium piano-stool complex towards DNA, we employed a presenter protein strategy based on the biotin-avidin technology. Guided by the X-ray structure of the assembly of streptavidin and a biotinylated piano-stool, we explored the formation of metallodrug-mediated ternary complexes with the presenter protein and DNA. The assemblies bound more strongly to telomere G-quadruplexes than to double-stranded DNA; chemo-genetic modifications (varying the complex or mutating the protein) modulated binding to these targets. We suggest that rational targeting of small molecules by presenter proteins could be exploited to bind metallodrugs to preferred macromolecular targets. PubMed: 20878805DOI: 10.1002/CHEM.201001573 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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