Thioredoxin-like domain of human κ class glutathione transferase reveals sequence homology and structure similarity to the θ class enzyme

Protein Science

Volumn 14, Issue 9, 2005, Pages 2361-2369

  Li, Jie ^a   Xia, Zongxiang ^a   Ding, Jianping ^b  

^a SHANGHAI INSTITUTE OF ORGANIC CHEMISTRY   (China)

^b Shanghai Jiao Tong University Affiliated Sixth People s Hospital   (China)

Author keywords

Active site; Crystal structure; Glutathione peroxidase; Glutathione sulfinate; Glutathione transferase; Thioredoxin like domain

Indexed keywords

DIMER; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE SULFINATE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE KAPPA; HYDROXYL GROUP; MONOMER; OXYGEN; SERINE; THIOREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CATALYST; CRYSTAL STRUCTURE; ENZYME PURIFICATION; ENZYME STRUCTURE; HUMAN; HUMAN CELL; HYDROGEN BOND; MITOCHONDRION; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN; THIOREDOXIN;

EID: 24344480389     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051463905     Document Type: Article

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