Multiple and distinct effects of mutations of Tyr122, Glu 123, Arg324, and Arg334 involved in interactions between the top part of second and fourth transmembrane helices in sarcoplasmic reticulum Ca2+-ATPase

Journal of Biological Chemistry

Volumn 279, Issue 3, 2004, Pages 2202-2210

  Yamasaki, Kazuo ^a   Daiho, Takashi ^a   Danko, Stefania ^a   Suzuki, Hiroshi ^a  

^a ASAHIKAWA MEDICAL COLLEGE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOLOGICAL MEMBRANES; HYDROGEN BONDS; HYDROLYSIS; SUBSTITUTION REACTIONS;

AROMATIC RINGS;

BIOCHEMISTRY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ARGININE; ASPARAGINE; CALCIUM ION; GLUTAMIC ACID; SARCOPLASMIC RETICULUM ADENOSINE TRIPHOSPHATASE (CALCIUM); TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CALCIUM TRANSPORT; CYTOPLASM; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; HYDROGEN BOND; HYDROLYSIS; HYDROPHOBICITY; ISOMERISM; MOLECULAR INTERACTION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ADENOSINE TRIPHOSPHATE; CALCIUM; CALCIUM-TRANSPORTING ATPASES; CELL MEMBRANE; CYTOPLASM; HYDROLYSIS; PROTEIN CONFORMATION; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA;

EID: 0347269062     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M309398200     Document Type: Article

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