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- W3098991002 endingPage "4075" @default.
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- W3098991002 abstract "The human multidrug transporter ABCG2 is required for physiological detoxification and mediates anticancer drug resistance. Here, we identify pivotal residues in the first intracellular loop (ICL1), constituting an intrinsic part of the transmission interface. The architecture includes a triple helical bundle formed by the hot spot helix of the nucleotide-binding domain, the elbow helix, and ICL1. We show here that the highly conserved ICL1 residues G462, Y463, and Y464 are essential for the proper cross talk of the closed nucleotide-binding domain dimer with the transmembrane domains. Hence, ICL1 acts as a molecular spring, triggering the conformational switch of ABCG2 before substrate extrusion. These data suggest that the ABCG2 transmission interface may offer therapeutic options for the treatment of drug-resistant malignancies." @default.
- W3098991002 created "2020-11-23" @default.
- W3098991002 creator A5016873011 @default.
- W3098991002 creator A5089656405 @default.
- W3098991002 date "2020-11-21" @default.
- W3098991002 modified "2023-09-24" @default.
- W3098991002 title "The first intracellular loop is essential for the catalytic cycle of the human ABCG2 multidrug resistance transporter" @default.
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