title: Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools.
abstract: P-glycoprotein is an ABC protein that functions as an efflux pump for multiple drugs, natural products and peptides. It is proposed to operate as a hydrophobic vacuum cleaner, expelling non-polar compounds from the membrane bilayer to the exterior, driven by the energy of ATP hydrolysis. The nucleotide-binding domains of P-glycoprotein appear to operate by an alternating sites mechanism to power drug transport. In recent years, purification and functional reconstitution of the protein has allowed the application of fluorescence spectroscopic techniques. This approach has led to insights into the structural architecture of the P-glycoprotein molecule, and a more detailed understanding of the way in which it interacts with nucleotides and drugs.
authors: Guelph-Waterloo Centre for Graduate Work in Chemistry and Biochemistry, Department of Chemistry and Biochemistry, University of Guelph, Guelph ON, Canada N1G 2W1. sharom@chembio.uoguelph.ca
authors: F J
authors: FJ
authors: Sharom
authors: R
authors: R
authors: Liu
authors: Q
authors: Q
authors: Qu
authors: Y
authors: Y
authors: Romsicki
mesh_terms: D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1 / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D000818:Animals; D018432:Drug Resistance, Multiple; D006801:Humans; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
chemical_list: D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1