Zn2+ inhibits the anion transport activity of band 3 by binding to its cytoplasmic tail.
Zn2+ can induce a conformational change of Band 3 with concomitant inhibition of its anion transport activity of human erythrocyte membrane vesicles only from the cytoplasmic side. The Zn2+ inhibition exhibits a dose-dependent manner with an apparent half maximal concentration of 50 microM ZnCl2 and can be reversed by 0.5 mM EDTA, but not by 1 mM dithiothreitol. The Zn2+ effect is specific and no similar inhibitory action could be observed by other divalent cations (Cu2+, Mn2+, Mg2+ or Sr2+).
National Laboratory of Biomacromolecules, Academia Sinica, Chaoyang District, Beijing, China.
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D001457:Anion Exchange Protein 1, Erythrocyte / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000838:Anions; D002413:Cations, Divalent; D003593:Cytoplasm; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D017136:Ion Transport; D007700:Kinetics; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013455:Sulfur / Q000737:chemistry; D015032:Zinc / Q000494:pharmacology*
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D002413:Cations, Divalent; D013455:Sulfur; D015032:Zinc