Nonequivalent Nucleotide Trapping in the Two Nucleotide Binding Folds of the Human Multidrug Resistance Protein MRP1

Multidrug resistance protein 1 (MRP1) and P-glycoprotein, which are ATP-dependent multidrug efflux pumps and involved in multidrug resistance of tumor cells, are members of the ATP binding cassette proteins and contain two nucleotide-binding folds (NBFs). P-glycoprotein hydrolyzes ATP at both NBFs,...

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Veröffentlicht in:	The Journal of biological chemistry 2000-06, Vol.275 (23), p.17626-17630
Hauptverfasser:	Nagata, Koh, Nishitani, Masahito, Matsuo, Michinori, Kioka, Noriyuki, Amachi, Teruo, Ueda, Kazumitsu
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Adenosine Triphosphate - pharmacokinetics Adenosine Triphosphate - pharmacology ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism Azides - pharmacokinetics Azides - pharmacology Binding Sites Cell Membrane - metabolism Drug Resistance, Multiple Etoposide - pharmacology Glutathione - pharmacology Glutathione Disulfide - pharmacology Humans KB Cells Kinetics MRP1 protein Multidrug Resistance-Associated Proteins nucleotides P-glycoprotein Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - metabolism Transfection Trypsin vanadate Vanadates - pharmacology
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