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http://purl.uniprot.org/citations/9587003http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9587003http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9587003http://www.w3.org/2000/01/rdf-schema#comment"Hydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.org/dc/terms/identifier"doi:10.1038/nsb0598-400"xsd:string
http://purl.uniprot.org/citations/9587003http://purl.org/dc/terms/identifier"doi:10.1038/nsb0598-400"xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Choi H.-J."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Choi H.-J."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Ryu S.-E."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Ryu S.-E."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Rhee S.G."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Rhee S.G."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Kang S.W."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Kang S.W."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Yang C.-H."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/author"Yang C.-H."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/pages"400-406"xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/pages"400-406"xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/title"Crystal structure of a novel human peroxidase enzyme at 2.0-A resolution."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/title"Crystal structure of a novel human peroxidase enzyme at 2.0-A resolution."xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/9587003http://purl.uniprot.org/core/volume"5"xsd:string