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Wu, Chyuan-Chuan; Li, Tsai-Kun; Farh, Lynn; Lin, Li-Ying; Lin, Te-Sheng; Yu, Yu-Jen; Yen, Tien-Jui; Chiang, Chia-Wang; Chan, Nei-Li
Science (American Association for the Advancement of Science), 07/2011, Letnik: 333, Številka: 6041Journal Article
Type II topoisomerases (TOP2s) resolve the topological problems of DNA by transiently cleaving both strands of a DNA duplex to form a cleavage complex through which another DNA segment can be transported. Several widely prescribed anticancer drugs increase the population of TOP2 cleavage complex, which leads to TOP2-mediated chromosome DNA breakage and death of cancer cells. We present the crystal structure of a large fragment of human TOP2β complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. The analysis of protein-drug interactions provides information applicable for developing an isoform-specific TOP2-targeting strategy.
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in: SICRIS
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