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  • Title: Binding of pyrene isothiocyanate to the E1ATP site makes the H4-H5 cytoplasmic loop of Na+/K+-ATPase rigid.
    Author: Linnertz H, Miksik I, Kvasnicka P, Bertoli E, Mazzanti L, Schoner W, Amler E.
    Journal: Eur J Biochem; 1998 Jan 15; 251(1-2):522-7. PubMed ID: 9492327.
    Abstract:
    1-Pyreneisothiocyanate was shown to be an inhibitor of Na+/K+-ATPase. Reverse-phase HPLC and activity studies indicated binding of 1-pyreneisothiocyanate at the H4-H5 loop of the alpha subunit and competition with the fluorescein 5'-isothiocyanate for the E1ATP site. While fluorescein 5'-isothiocyanate, the fluorescent ATP pseudo-analog, was shown to be immobilized at the E1ATP site, there was no possibility to draw any conclusion about the flexibility of the E1ATP site due to its short lifetime. Employing 1-pyreneisothiocyanate as a long-lived fluorophore and a label for the E1ATP site, we found that the ATP-binding site of Na+/K+-ATPase and, in fact, the whole large intracellularly exposed H4-H5 loop of the catalytic alpha subunit is rigid and rotationally immobilized. This has important consequences for the molecular mechanism of the transport function.
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