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- W2157393167 abstract "P-glycoprotein (P-gp) detoxifies cells by exporting hundreds of chemically unrelated toxins but has been implicated in multidrug resistance (MDR) in the treatment of cancers. Substrate promiscuity is a hallmark of P-gp activity, thus a structural description of poly-specific drug-binding is important for the rational design of anticancer drugs and MDR inhibitors. The x-ray structure of apo P-gp at 3.8 angstroms reveals an internal cavity of ∼6000 angstroms cubed with a 30 angstrom separation of the two nucleotide-binding domains. Two additional P-gp structures with cyclic peptide inhibitors demonstrate distinct drug-binding sites in the internal cavity capable of stereoselectivity that is based on hydrophobic and aromatic interactions. Apo and drug-bound P-gp structures have portals open to the cytoplasm and the inner leaflet of the lipid bilayer for drug entry. The inward-facing conformation represents an initial stage of the transport cycle that is competent for drug binding." @default.
- W2157393167 created "2016-06-24" @default.
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- W2157393167 date "2009-03-27" @default.
- W2157393167 modified "2023-10-09" @default.
- W2157393167 title "Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding" @default.
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- W2157393167 doi "https://doi.org/10.1126/science.1168750" @default.
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