1k4q

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[[Image:1k4q.jpg|left|200px]]
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{{Seed}}
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[[Image:1k4q.png|left|200px]]
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{{STRUCTURE_1k4q| PDB=1k4q | SCENE= }}
{{STRUCTURE_1k4q| PDB=1k4q | SCENE= }}
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'''Human Glutathione Reductase Inactivated by Peroxynitrite'''
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===Human Glutathione Reductase Inactivated by Peroxynitrite===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11705998 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11705998}}
==About this Structure==
==About this Structure==
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[[Category: Flavoenzyme]]
[[Category: Flavoenzyme]]
[[Category: Nitrotyrosine]]
[[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 Wed Jul 2 09:46:13 2008''

Revision as of 06:46, 2 July 2008

Image:1k4q.png

Template:STRUCTURE 1k4q

Human Glutathione Reductase Inactivated by Peroxynitrite

Template:ABSTRACT PUBMED 11705998

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

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