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1prx

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[[Image:1prx.gif|left|200px]]
[[Image:1prx.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1prx", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>
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{{STRUCTURE_1prx| PDB=1prx | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1prx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prx OCA], [http://www.ebi.ac.uk/pdbsum/1prx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1prx RCSB]</span>
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'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''
'''HORF6 A NOVEL HUMAN PEROXIDASE ENZYME'''
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[[Category: Ryu, S E.]]
[[Category: Ryu, S E.]]
[[Category: Yang, C H.]]
[[Category: Yang, C H.]]
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[[Category: antioxidant]]
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[[Category: Antioxidant]]
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[[Category: cellular signaling]]
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[[Category: Cellular signaling]]
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[[Category: horf6]]
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[[Category: Horf6]]
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[[Category: hydrogen peroxide]]
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[[Category: Hydrogen peroxide]]
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[[Category: peroxiredoxin]]
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[[Category: Peroxiredoxin]]
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[[Category: redox regulation]]
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[[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 Mar 30 23:03:44 2008''
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Revision as of 02:25, 3 May 2008

Template:STRUCTURE 1prx

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME


Overview

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.

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 Page seeded by OCA on Sat May 3 05:25:00 2008

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