2icq: Difference between revisions

Revision as of 00:29, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2icq.png

Template:STRUCTURE 2icq

urate oxidase under 2.0 MPa pressure of nitrous oxideurate oxidase under 2.0 MPa pressure of nitrous oxide

Template:ABSTRACT PUBMED 17028130

About this StructureAbout this Structure

2ICQ is a Single protein structure of sequence from Aspergillus flavus. Full crystallographic information is available from OCA.

ReferenceReference

Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action., Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH, Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130

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OCA

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-'''urate oxidase under 2.0 MPa pressure of nitrous oxide'''
+===urate oxidase under 2.0 MPa pressure of nitrous oxide===
-==Overview==
+<!--
-In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia.
+The line below this paragraph, {{ABSTRACT_PUBMED_17028130}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17028130}}
 ==About this Structure==
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 [[Category: T-fold domain]]
 [[Category: Uric acid degradation]]
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