The sodium pump. Its molecular properties and mechanics of ion transport

European Journal of Biochemistry

Volumn 269, Issue 10, 2002, Pages 2424-2433

  Scheiner Bobis, Georgios ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

Author keywords

ATPase; Ion transport; Ouabain; P type; Palytoxin

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE INHIBITOR; DIGITALIS; OUABAIN; PALYTOXIN; PHOSPHATASE; POTASSIUM ION; PROTEIN SUBUNIT; SODIUM ION;

ACTIVE TRANSPORT; CATALYSIS; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYMOLOGY; HUMAN; HYDROLYSIS; ION TRANSPORT; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; SHORT SURVEY;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CATALYSIS; CELL MEMBRANE; ENZYME INHIBITORS; FORECASTING; HYDROLYSIS; ION TRANSPORT; NA(+)-K(+)-EXCHANGING ATPASE; POTASSIUM;

DIGITALIS; STROPHANTHUS GRATUS;

EID: 0036098782     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.02909.x     Document Type: Short Survey

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33. 2+) ions accompanies the E1 → E2 conformational change
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37. Site-directed mutagenesis of a predicted cation binding site of Na,K-ATPase
38. +-ATPase displays low cation affiity and catalyses ATP hydrolysis at a high rate in the absence of potassium ions
39. Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues
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