2IE7

Annexin V under 2.0 MPa pressure of nitrous oxide

Summary for 2IE7

• Entry DOI: 10.2210/pdb2ie7/pdb
• Related: 2IE6
• Descriptor: Annexin A5, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: calcium binding protein, phospholipid binding protein, membrane binding protein, protein and metal binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 36410.09

Authors

Colloc'h, N.,Sopkova-de Oliveira Santos, J.,Prange, T.,Brisson, A.,Langlois d'Estainto, B.,Gallois, B. (deposition date: 2006-09-18, release date: 2007-02-06, Last modification date: 2023-10-25)

Primary citation

Colloc'h, N.,Sopkova-de Oliveira Santos, J.,Retailleau, P.,Langlois d'Estainto, B.,Gallois, B.,Brisson, A.,Risso, J.J.,Lemaire, M.,Abraini, J.H.
Protein Crystallography under Xenon and Nitrous Oxide Pressure: Comparison with In Vivo Pharmacology Studies and Implications for the Mechanism of Inhaled Anesthetic Action
Biophys.J., 92:217-224, 2007

PubMed Abstract: 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.

PubMed: 17028130
DOI: 10.1529/biophysj.106.093807

Experimental method

X-RAY DIFFRACTION (1.75 Å)