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- W2913173637 abstract "To transport or not to transport Therapeutic drug delivery into cells is complicated by membrane proteins like ABCB1 (also termed P-glycoprotein) that shuttle diverse compounds out of cells. Alam et al. determined high-resolution cryo–electron microscopy structures of ABCB1 bound either to a substrate, the cancer drug Taxol, or to the ABCB1 inhibitor zosuquidar. The conformational changes that facilitate drug transport are caused by hydrolysis of adenosine triphosphate (ATP). The structures show that, although Taxol and zosquidar bind to the same site, subtle structural differences lead to altered conformations of the nucleotide binding domains that are responsible for ATP hydrolysis. Science , this issue p. 753" @default.
- W2913173637 created "2019-02-21" @default.
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- W2913173637 date "2019-02-15" @default.
- W2913173637 modified "2023-10-17" @default.
- W2913173637 title "Structural insight into substrate and inhibitor discrimination by human P-glycoprotein" @default.
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- W2913173637 doi "https://doi.org/10.1126/science.aav7102" @default.
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