1k4q

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[[Image:1k4q.jpg|left|200px]]
[[Image:1k4q.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1k4q |SIZE=350|CAPTION= <scene name='initialview01'>1k4q</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1k4q", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1k4q| PDB=1k4q | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4q OCA], [http://www.ebi.ac.uk/pdbsum/1k4q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4q RCSB]</span>
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}}
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'''Human Glutathione Reductase Inactivated by Peroxynitrite'''
'''Human Glutathione Reductase Inactivated by Peroxynitrite'''
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[[Category: Scheiwein, M.]]
[[Category: Scheiwein, M.]]
[[Category: Schirmer, R H.]]
[[Category: Schirmer, R H.]]
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[[Category: flavoenzyme]]
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[[Category: Flavoenzyme]]
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[[Category: nitrotyrosine]]
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[[Category: Nitrotyrosine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:18:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:27 2008''
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Revision as of 19:18, 2 May 2008

Image:1k4q.jpg

Template:STRUCTURE 1k4q

Human Glutathione Reductase Inactivated by Peroxynitrite


Overview

As part of our studies on the nitric oxide-related pathology of cerebral malaria, we show that the antioxidative enzyme glutathione reductase (GR) is inactivated by peroxynitrite, with GR from the malarial parasite Plasmodium falciparum being more sensitive than human GR. The crystal structure of modified human GR at 1.9-A resolution provides the first picture of protein inactivation by peroxynitrite and reveals that this is due to the exclusive nitration of 2 Tyr residues (residues 106 and 114) at the glutathione disulfide-binding site. The selective nitration explains the impairment of binding the peptide substrate and thus the nearly 1000-fold decrease in catalytic efficiency (k(cat)/K(m)) of glutathione reductase observed at physiologic pH. By oxidizing the catalytic dithiol to a disulfide, peroxynitrite itself can act as a substrate of unmodified and bisnitrated P. falciparum glutathione reductase.

About this Structure

1K4Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite., Savvides SN, Scheiwein M, Bohme CC, Arteel GE, Karplus PA, Becker K, Schirmer RH, J Biol Chem. 2002 Jan 25;277(4):2779-84. Epub 2001 Nov 8. PMID:11705998 Page seeded by OCA on Fri May 2 22:18:20 2008

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