Importance of Glu282 in transmembrane segment M3 of the Na+,K+-ATPase for control of cation interaction and conformational changes

Journal of Biological Chemistry

Volumn 277, Issue 41, 2002, Pages 38607-38617

  Toustrup Jensen, Mads ^a   Vilsen, Bente ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CATALYSIS; CONFORMATIONS; ENZYMES; HYDROLYSIS; MOLECULAR BIOLOGY;

MUTATIONS;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ALANINE; CATION; GLUTAMINE; GLYCINE; POTASSIUM ION; SODIUM ION;

AMINO ACID TRANSPORT; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME STRUCTURE; EQUILIBRIUM CONSTANT; HYDROLYSIS; MEMBRANE STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; CATALYTIC DOMAIN; ENZYME ACTIVATION; ENZYME INHIBITORS; GLUTAMIC ACID; ISOENZYMES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; PHOSPHORYLATION; POTASSIUM; PROTEIN STRUCTURE, TERTIARY; RATS; SODIUM; TIME FACTORS; VANADATES;

ANIMALIA;

EID: 0037064028     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M203665200     Document Type: Article

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