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Volumn 98, Issue 17, 2001, Pages 9533-9538
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Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme
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Author keywords
[No Author keywords available]
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Indexed keywords
FLAVINE ADENINE NUCLEOTIDE;
GLUTATHIONE DISULFIDE;
GLUTATHIONE REDUCTASE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
SELENOCYSTEINE;
THIOREDOXIN REDUCTASE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CONFORMATIONAL TRANSITION;
ELECTRON TRANSPORT;
ENZYME ACTIVE SITE;
ENZYME MECHANISM;
ENZYME STRUCTURE;
GENETIC CONSERVATION;
MAMMAL;
PRIORITY JOURNAL;
PROTEIN PROTEIN INTERACTION;
REDUCTION;
X RAY CRYSTALLOGRAPHY;
AMINO ACID SEQUENCE;
ANIMALS;
BINDING SITES;
CATALYSIS;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
EVOLUTION, MOLECULAR;
FLAVIN-ADENINE DINUCLEOTIDE;
GLUTATHIONE REDUCTASE;
HYDROGEN BONDING;
MAMMALS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
NADP;
OXIDATION-REDUCTION;
PROKARYOTIC CELLS;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
RATS;
SELENOCYSTEINE;
SEQUENCE HOMOLOGY, AMINO ACID;
SPECIES SPECIFICITY;
THIOREDOXIN REDUCTASE (NADPH);
MAMMALIA;
PROKARYOTA;
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EID: 0035859927
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.171178698 Document Type: Article |
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Times cited : (310)
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References (39)
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