2icq: Difference between revisions

Revision as of 18:51, 21 February 2008

urate oxidase under 2.0 MPa pressure of nitrous oxide

OverviewOverview

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.

About this StructureAbout this Structure

2ICQ is a Single protein structure of sequence from Aspergillus flavus with , , and as ligands. Active as Urate oxidase, with EC number 1.7.3.3 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

Page seeded by OCA on Thu Feb 21 17:51:20 2008

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-[[Image:2icq.jpg|left|200px]]<br /><applet load="2icq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2icq.jpg|left|200px]]<br /><applet load="2icq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2icq, resolution 1.750&Aring;" />
 '''urate oxidase under 2.0 MPa pressure of nitrous oxide'''<br />
 ==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.
+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.
 ==About this Structure==
-ICQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with ACE, AZA, CYS and N2O as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ICQ OCA].
+ICQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=AZA:'>AZA</scene>, <scene name='pdbligand=CYS:'>CYS</scene> and <scene name='pdbligand=N2O:'>N2O</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ICQ OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Urate oxidase]]
-[[Category: Abraini, J.H.]]
+[[Category: Abraini, J H.]]
 [[Category: Prange, T.]]
 [[Category: Retailleau, P.]]
-[[Category: Santos, J.Sopkova-de.Oliveira.]]
+[[Category: Santos, J Sopkova-de Oliveira.]]
-[[Category: h, N.Colloc.]]
+[[Category: h, N Colloc.]]
 [[Category: ACE]]
 [[Category: AZA]]
@@ Line 27: / Line 27: @@
 [[Category: uric acid degradation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:14:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:20 2008''