We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2ie6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ie6.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ie6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ie6| PDB=2ie6 | SCENE= }}
{{STRUCTURE_2ie6| PDB=2ie6 | SCENE= }}
-
'''Annexin V under 2.0 MPa pressure of xenon'''
+
===Annexin V under 2.0 MPa pressure of xenon===
-
==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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17028130 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17028130}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Membrane binding protein]]
[[Category: Membrane binding protein]]
[[Category: Phospholipid binding protein]]
[[Category: Phospholipid binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:23:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:16:12 2008''

Revision as of 23:16, 27 July 2008

Image:2ie6.png

Template:STRUCTURE 2ie6

Annexin V under 2.0 MPa pressure of xenon

Template:ABSTRACT PUBMED 17028130

About this Structure

2IE6 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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 Mon Jul 28 02:16:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ie6"
Personal tools