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Titolo:
Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools
Autore:
Sharom, FJ; Liu, RH; Qu, Q; Romsicki, Y;
Indirizzi:
Univ Guelph, Guelph Waterloo Ctr Grad Work Chem & Biochem, Dept Chem & Biochem, Guelph, ON N1G 2W1, Canada Univ Guelph Guelph ON Canada N1G 2W1 Biochem, Guelph, ON N1G 2W1, Canada
Titolo Testata:
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
fascicolo: 3, volume: 12, anno: 2001,
pagine: 257 - 265
SICI:
1084-9521(200106)12:3<257:ETSAFO>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE-BINDING DOMAIN; HAMSTER OVARY CELLS; DRUG TRANSPORT; ATPASE ACTIVITY; PHOSPHATIDYLCHOLINE TRANSLOCASE; ABC TRANSPORTERS; PLASMA-MEMBRANE; RECONSTITUTION; PURIFICATION; HYDROLYSIS;
Keywords:
multidrug resistance; ABC superfamily; substrate binding; fluorescence quenching; resonance energy transfer;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Sharom, FJ Univ Guelph, Guelph Waterloo Ctr Grad Work Chem & Biochem, DeptChem & Biochem, Guelph, ON N1G 2W1, Canada Univ Guelph Guelph ON Canada N1G 2W1 uelph, ON N1G 2W1, Canada
Citazione:
F.J. Sharom et al., "Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools", SEM CELL D, 12(3), 2001, pp. 257-265

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 nucleo tides and drugs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 23:26:18