Ontology highlight
ABSTRACT:
SUBMITTER: Sanchez-Rodriguez JE
PROVIDER: S-EPMC4457281 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Sánchez-Rodríguez Jorge E JE Khalili-Araghi Fatemeh F Miranda Pablo P Roux Benoît B Holmgren Miguel M Bezanilla Francisco F
Journal of molecular biology 20150128 6 Pt B
With the use of the energy of ATP hydrolysis, the Na+/K+-ATPase is able to transport across the cell membrane Na+ and K+ against their electrochemical gradients. The enzyme is strongly inhibited by ouabain and its derivatives, some that are therapeutically used for patients with heart failure (cardiotonic steroids). Using lanthanide resonance energy transfer, we trace here the conformational changes occurring on the external side of functional Na+/K+-ATPases induced by the binding of ouabain. Ch ...[more]