Ouabain affinity determining residues lie close to the Na/K pump ion pathway

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 33, 2006, Pages 12613-12618

  Artigas, Pablo ^a   Gadsby, David C ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Cysteine modification; Electrostatic mechanism; Na,K atpase; Palytoxin; Single channel conductance

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CARDIOTONIC AGENT; CYSTEINE; ION CHANNEL; MARINE TOXIN; METHANETHIOSULFONATE; OUABAIN; PALYTOXIN; STEROID; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CHANNEL GATING; CONTROLLED STUDY; ELECTRICITY; ELECTROPHYSIOLOGY; GENE EXPRESSION; GENE SILENCING; ION CONDUCTANCE; ION TRANSPORT; NONHUMAN; OOCYTE; PATCH CLAMP; POINT MUTATION; PRIORITY JOURNAL; SURFACE CHARGE; XENOPUS;

ACRYLAMIDES; AMINO ACID SEQUENCE; ANIMALS; CNIDARIAN VENOMS; ENZYME INHIBITORS; IONS; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NA(+)-K(+)-EXCHANGING ATPASE; OUABAIN; PATCH-CLAMP TECHNIQUES; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SEQUENCE ALIGNMENT; XENOPUS LAEVIS;

ANIMALIA; STROPHANTHUS GRATUS;

EID: 33747584895     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0602720103     Document Type: Article

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