Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli

Journal of Biological Chemistry

Volumn 280, Issue 26, 2005, Pages 24553-24561

  Fladvad, Malin ^a   Bellanda, Massimo ^b   Fernandes, Aristi Potamitou ^a   Mammi, Stefano ^b   Vlamis Gardikas, Alexios ^a   Holmgren, Arne ^a   Sunnerhagen, Maria ^a,c  

^a KAROLINSKA INSTITUTE   (Sweden)

^b UNIVERSITY OF PADOVA   (Italy)

^c LINKÖPING UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; GENES; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE; OXIDATION; PROTEINS; SUBSTRATES; YEAST;

GLUTAREDOXIN PROTEINS; LIGAND BINDING; MOLECULAR MAPPING; OXIDATIVE STRESS;

ESCHERICHIA COLI;

DITHIOL DERIVATIVE; GLUTAREDOXIN; GLUTAREDOXIN 3; GLUTAREDOXIN 4; GLUTATHIONE; THIOREDOXIN; UBIQUITIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BACTERIAL GENOME; BETA SHEET; BINDING SITE; CHEMICAL REACTION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; EUKARYOTE; GENE MAPPING; GENETIC CONSERVATION; GLUTATHIONYLATION; HYDROPHOBICITY; LIGAND BINDING; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION MASS SPECTROMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROKARYOTE; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; YEAST;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CYSTEINE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENOME, BACTERIAL; GLUTATHIONE; HUMANS; HYDROGEN BONDING; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUBSTRATE SPECIFICITY; THIOREDOXIN; THIOREDOXIN REDUCTASE (NADPH);

CELLULAR ORGANISMS; ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA;

EID: 21644481715     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M500679200     Document Type: Article

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