Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B

Journal of Biological Chemistry

Volumn 285, Issue 9, 2010, Pages 6327-6336

  LeShane, Erik S ^a   Shinde, Ujwal ^a   Walker, Joel M ^a   Barry, Amanda N ^b   Blackburn, Ninian J ^a   Ralle, Martina ^a   Lutsenko, Svetlana ^a,b  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER BINDING; COPPER HOMEOSTASIS; CYTOSOLIC; INTERDOMAIN COMMUNICATION; METAL BINDING DOMAIN; METAL-BINDING SITES; N-TERMINAL DOMAINS; N-TERMINALS; OXIDATION STATE; REDOX STATUS; REDUCED-STATE; REGULATORY PROTEIN; SIGNAL INTEGRATION; TIGHT COUPLING;

BINDING ENERGY; BIOCHEMISTRY; CONFORMATIONS; COPPER; HYDROGEN BONDS; OXIDATION;

BINDING SITES;

ALANINE; CYSTEINE; METAL BINDING DOMAIN 2 PROTEIN; METAL BINDING DOMAIN 3 PROTEIN; METAL BINDING DOMAIN 4 PROTEIN; METAL BINDING DOMAIN 6 PROTEIN; REGULATOR PROTEIN; SERINE; UNCLASSIFIED DRUG; WILSON DISEASE PROTEIN; ADENOSINE TRIPHOSPHATASE; CATION TRANSPORT PROTEIN; COPPER;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; GENE MUTATION; HYDROGEN BOND; METAL BINDING; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; CHEMISTRY; GENETICS; HUMAN; METABOLISM; OXIDATION REDUCTION REACTION; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATASES; BINDING SITES; CATION TRANSPORT PROTEINS; COPPER; CYSTEINE; HUMANS; HYDROGEN BONDING; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION;

EID: 77949890049     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.074633     Document Type: Article

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