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      Binding of ouabain and marinobufagenin leads to different structural changes in Na,K-ATPase and depends on the enzyme conformation.

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          Abstract

          Ion pump, Na,K-ATPase specifically binds cardiotonic steroids (CTS), which leads to inhibition of the enzyme activity and activation of signaling network in the cell. We have studied interaction of Na,K-ATPase with CTS of two different types - marinobufagenin and ouabain. We have shown that both CTS inhibit activity of Na,K-ATPase with the same Ki values, but binding of ouabain is sensitive to the conformation of Na,K-ATPase while binding of marinobufagenin is not. Furthermore, binding of ouabain and marinobufagenin results in different structural changes in Na,K-ATPase. Our data allow to explain the diversity of effects on the receptor function of Na,K-ATPase caused by different types of CTS.

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          Author and article information

          Journal
          FEBS Lett.
          FEBS letters
          Elsevier BV
          1873-3468
          0014-5793
          Sep 14 2015
          : 589
          : 19 Pt B
          Affiliations
          [1 ] Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Vavilov Str. 32, Moscow, Russia; Faculty of Biology, M.V. Lomonosov Moscow State University, 119234 Moscow, Russia.
          [2 ] Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Vavilov Str. 32, Moscow, Russia.
          [3 ] Faculty of Biology, M.V. Lomonosov Moscow State University, 119234 Moscow, Russia.
          [4 ] Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Vavilov Str. 32, Moscow, Russia. Electronic address: aamakarov@eimb.ru.
          Article
          S0014-5793(15)00710-3
          10.1016/j.febslet.2015.08.011
          26297827
          8e790914-5517-41cd-8e76-2e2d5a68139f
          History

          Cardiotonic steroid,Conformational change,Isothermal titration calorimetry,Na,K-ATPase,Protein fluorescent label,Protein-ligand binding

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