2wpu | pdb_00002wpu

Chaperoned ruthenium metallodrugs that recognize telomeric DNA

spinqualitylabelsall models 2wpu, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wpu is a 1 chain structure with sequence from As 4.1583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, KYT, SO4 Related: 1swh, 2bc3, 1vwq, 1sre, 1swf, 2rtb, 1lcw, 1hxz, 1swp, 1rxj, 1swe, 1mm9, 2rto, 1swa, 2rtr, 2rtd, 1stp, 1n43, 2izh, 1sri, 1slf, 1swc, 1vwr, 1swl, 1ndj, 1str, 1slg, 1vwm, 1swd, 1swq, 1swu, 1i9h, 1swj, 2rtj, 2rtl, 2iza, 1vwn, 1vwk, 1vwg, 1moy, 1sts, 1hqq, 1vwi, 2izg, 1swg, 2izb, 1swk, 2izk, 1luq, 1sws, 1n4j, 2izd, 1lcv, 1swt, 1df8, 1vwl, 1vwb, 2rtk, 1srj, 1kl3, 2rti, 2izf, 1swr, 2rth, 2rtm, 2izi, 1vwf, 1vwh, 1pts, 1mk5, 1hxl, 2f01, 1vwd, 1nc9, 1sle, 1vwj, 2ize, 2rtf, 2rtp, 1n9y, 1n9m, 1hy2, 1lcz, 1nqm, 1vwa, 2izl, 1kl5, 2izc, 1mep, 1sld, 1rxh, 1rsu, 1vwc, 1nbx, 1srh, 2izj, 1rst, 1kff, 1srg, 1vwe, 2rtg, 1rxk, 1kl4, 1srf, 2rtq, 2rte, 1swb, 1vwo, 2rta, 2rtc, 2rtn, 1swo, 1swn, 1n7y, 1vwp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMed 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. Chemo-Genetic Optimization of DNA Recognition by Metallodrugs using a Presenter-Protein Strategy.,Zimbron JM, Sardo A, Heinisch T, Wohlschlager T, Gradinaru J, Massa C, Schirmer T, Creus M, Ward TR Chemistry. 2010 Sep 28. PMID:20878805 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin 3D structures

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