Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution

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dc.contributor.authorHee Jeong Choi-
dc.contributor.authorSang Won Kang-
dc.contributor.authorChul Hak Yang-
dc.contributor.authorSue Goo Rhee-
dc.contributor.authorSeong Eon Ryu-
dc.date.accessioned2017-04-19T08:55:33Z-
dc.date.available2017-04-19T08:55:33Z-
dc.date.issued1998-
dc.identifier.issn1072-8368-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4495-
dc.description.abstractHydrogen 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.-
dc.publisherSpringer-Nature Pub Group-
dc.titleCrystal structure of a novel human peroxidase enzyme at 2.0 Å resolution-
dc.title.alternativeCrystal structure of a novel human peroxidase enzyme at 2.0 Å resolution-
dc.typeArticle-
dc.citation.titleNature Structural & Molecular Biology-
dc.citation.number5-
dc.citation.endPage406-
dc.citation.startPage400-
dc.citation.volume5-
dc.contributor.affiliatedAuthorHee Jeong Choi-
dc.contributor.affiliatedAuthorSeong Eon Ryu-
dc.contributor.alternativeName최희정-
dc.contributor.alternativeName강상원-
dc.contributor.alternativeName양철학-
dc.contributor.alternativeName이서구-
dc.contributor.alternativeName류성언-
dc.identifier.bibliographicCitationNature Structural & Molecular Biology, vol. 5, no. 5, pp. 400-406-
dc.identifier.doi10.1038/nsb0598-400-
dc.description.journalClassY-
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