Multiple transport-active binding sites are available for a single substrate on human P-glycoprotein (ABCB1)

• Main Authors: Chufan E.E., Kapoor K., Sim H.-M., Singh S., Talele T.T., Durell S.R., Ambudkar S.A.
• Other Authors: PHARMACY
• Format: Article
• Published: 2019
• Subjects: 5' fluorosulfonylbenzoyl 5' adenosine; adenosine derivative; adenosine triphosphate; cyclosporin A; cysteine; glutamine; membrane protein; multidrug resistance protein 1; mutant protein; paclitaxel; phenylalanine; sulfur derivative; tariquidar; tyrosine; unclassified drug; valine; valinomycin; amino acid substitution; article; baculovirus expression system; cell surface; controlled study; drug binding site; drug transport; HeLa cell; human; human cell; hydrolysis; insect cell; mammal cell; molecular docking; molecular model; nonhuman; protein aggregation; protein domain; protein expression; residue analysis; sequence homology; site directed mutagenesis; Adenosine Triphosphatases; Adenosine Triphosphate; Binding Sites; Cell Line, Tumor; Fluorescent Dyes; Gene Expression; HeLa Cells; Humans; Hydrolysis; Models, Molecular; Molecular Docking Simulation; Mutagenesis, Site-Directed; P-Glycoprotein; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; Transduction, Genetic
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161451
• Institution: National University of Singapore

10.1371/journal.pone.0082463