Structural and functional asymmetry of the nucleotide-binding domains of P-glycoprotein investigated by attenuated total reflection Fourier transform infrared spectroscopy.

Abstract excerpt

The dynamic changes occurring during the catalytic cycle of MDR3 P-glycoprotein (Pgp) and the role of each nucleotide-binding domain (NBD) in the transport process were investigated using attenuated total reflection Fourier transform infrared spectroscopy. For this purpose, wild-type Pgp and two mutations of homologous residues in each NBD were studied. On the one hand, we demonstrate here that, during its...

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