1prx

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[[Image:1prx.gif|left|200px]]
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{{STRUCTURE_1prx| PDB=1prx | SCENE= }}
{{STRUCTURE_1prx| PDB=1prx | SCENE= }}
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'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''
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===HORF6 A NOVEL HUMAN PEROXIDASE ENZYME===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9587003 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9587003}}
==About this Structure==
==About this Structure==
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[[Category: Peroxiredoxin]]
[[Category: Peroxiredoxin]]
[[Category: Redox regulation]]
[[Category: Redox regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:25:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:11:35 2008''

Revision as of 17:11, 27 July 2008

Image:1prx.png

Template:STRUCTURE 1prx

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

Template:ABSTRACT PUBMED 9587003

About this Structure

1PRX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution., Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE, Nat Struct Biol. 1998 May;5(5):400-6. PMID:9587003

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