A mutational study in the transmembrane domain of Ccc2p, the yeast Cu(I)-ATPase, shows different roles for each Cys-Pro-Cys cysteine

Journal of Biological Chemistry

Volumn 279, Issue 25, 2004, Pages 25986-25994

  Lowe, Jennifer ^a   Vieyra, Adalberto ^a   Catty, Patrice ^b   Guillain, Florent ^b   Mintz, Elisabeth ^b   Cuillel, Martine ^a  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b CEA GRENOBLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; COPPER; DISEASE CONTROL; ENZYMES; MUTAGENESIS; VIRUSES; YEAST;

MUTATION; TRANSMEMBRANE DOMAIN;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (COPPER); CCC2P PROTEIN; COPPER; CYSTEINE; MEMBRANE PROTEIN; PROLINE; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACULOVIRUS EXPRESSION SYSTEM; CATION TRANSPORT; CONTROLLED STUDY; DEPHOSPHORYLATION; DISSOCIATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; GENE MUTATION; GENETIC COMPLEMENTATION; HUMAN; INSECT CELL; MENKES SYNDROME; METAL BINDING; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN VARIANT; SEQUENCE HOMOLOGY; WILSON DISEASE; YEAST;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BACULOVIRIDAE; BIOLOGICAL TRANSPORT; CATION TRANSPORT PROTEINS; CELL LINE; CELL MEMBRANE; CHELATING AGENTS; COPPER; CYSTEINE; CYTOPLASM; DOSE-RESPONSE RELATIONSHIP, DRUG; GENETIC COMPLEMENTATION TEST; INSECTS; LIGANDS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTATION; PHENANTHROLINES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; QUINOLINES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TEMPERATURE; TIME FACTORS;

INSECTA; UNIDENTIFIED BACULOVIRUS;

EID: 2942700106     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M308736200     Document Type: Article

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