Functional Role of Arginine 375 in Transmembrane Helix 6 of Multidrug Resistance Protein 4 (MRP4/ABCC4)

@article{ElSheikh2008FunctionalRO,
  title={Functional Role of Arginine 375 in Transmembrane Helix 6 of Multidrug Resistance Protein 4 (MRP4/ABCC4)},
  author={A. El-Sheikh and J. J. van den Heuvel and E. Krieger and F. Russel and J. B. Koenderink},
  journal={Molecular Pharmacology},
  year={2008},
  volume={74},
  pages={964 - 971}
}
Multidrug resistance protein (MRP) 4 transports a variety of endogenous and xenobiotic organic anions. MRP4 is widely expressed in the body and specifically localized to the renal apical proximal tubule cell membrane, where it mediates the excretion of these compounds into urine. To characterize the MRP4 substrate-binding site, the amino acids Phe368, Phe369, Glu374, Arg375, and Glu378 of transmembrane helix 6, and Arg998 of helix 12, localized in the intracellular half of the central pore… Expand
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Localization of putative binding sites for cyclic guanosine monophosphate and the anti-cancer drug 5-fluoro-2′-deoxyuridine-5′-monophosphate on ABCC11 in silico models
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Localization of putative binding sites for cyclic guanosine monophosphate and the anti-cancer drug 5-fluoro-2 [ prime ]-deoxyuridine-5 [ prime ]-monophosphate on ABCC 11 in silico models
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