2ie6: Difference between revisions

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[[Image:2ie6.gif|left|200px]]
[[Image:2ie6.gif|left|200px]]


{{Structure
<!--
|PDB= 2ie6 |SIZE=350|CAPTION= <scene name='initialview01'>2ie6</scene>, resolution 1.830&Aring;
The line below this paragraph, containing "STRUCTURE_2ie6", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>
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|ACTIVITY=
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|GENE=
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|DOMAIN=
{{STRUCTURE_2ie6| PDB=2ie6  | SCENE= }}  
|RELATEDENTRY=[[2ie7|2IE7]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ie6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ie6 OCA], [http://www.ebi.ac.uk/pdbsum/2ie6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ie6 RCSB]</span>
}}


'''Annexin V under 2.0 MPa pressure of xenon'''
'''Annexin V under 2.0 MPa pressure of xenon'''
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[[Category: Prange, T.]]
[[Category: Prange, T.]]
[[Category: Santos, J Sopkova-de Oliveira.]]
[[Category: Santos, J Sopkova-de Oliveira.]]
[[Category: h, N Colloc.]]
[[Category: H, N Colloc.]]
[[Category: calcium binding protein]]
[[Category: Calcium binding protein]]
[[Category: membrane binding protein]]
[[Category: Membrane binding protein]]
[[Category: phospholipid binding protein]]
[[Category: Phospholipid binding protein]]
 
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Revision as of 07:23, 4 May 2008

File:2ie6.gif

Template:STRUCTURE 2ie6

Annexin V under 2.0 MPa pressure of xenon


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

2IE6 is a Single protein structure of sequence from Rattus norvegicus. 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 Sun May 4 07:23:48 2008

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