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Transcript
General structure of ABC membrane drug efflux pumps. A) (left) Shown is a linear topological cartoon of the core structure of ABC transporters such as Pglycoprotein showing the 2 cytoplasmic nucleotide-binding domains (NBDs) and 12 transmembrane (TM) helices (here shown as cylinders) equally distributed between 2 membrane-spanning domains (MSDs). (right) Shown is a 3D homology model of the core structure of MRP1 (lacking MSD0, see Fig 19–5B) generated using the crystal structure of Staphylococcus aureus Sav1866 as template (Hollenstein et al, 2007; DeGorter et al, 2008). The α-carbon backbone in ribbon representation of the core structure (MSD1-NBD1-MSD2-NBD2) is viewed from the plane perpendicular to the membrane bilayer (DeGorter et al, 2008). Homology models of P-glycoprotein, MRP4 and other ABC transporters look very similar. The 2 NBDs form a "sandwich" dimer for Source: Drug Resistance, The Basic Science of Oncology, 5e the effective binding and hydrolysis of 2 molecules of ATP, providing the energy for the transport process. Signaling between the MSDs (translocation Citation: IF, Hill RG, Harrington L. The Basicfor Science of Oncology, 5e; by 2016 Available at: http://mhmedical.com/ pathway through the Tannock membrane) andRP, theBristow NBDs (which provide the energy transport) is mediated specific sequences in the cytoplasmic loops. Accessed: May 10, 2017 Substrates that enter the cell by diffusion or active transport, or are formed in the cell by conjugation, are thought to be exported from the cell either directly Copyright McGraw-Hill rights reserved through the pore from © the2017 cytoplasm, or in Education. the case ofAll hydrophobic drugs, are taken up from the inner leaflet of the membrane lipid bilayer. B) Domain organization of ABC transporter drug (and drug metabolite) efflux pumps implicated in drug resistance in malignant cells. P-glycoprotein and the MRPs are