Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations.

Détails

ID Serval
serval:BIB_EF97A568A73D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations.
Périodique
Biochemistry
Auteur(s)
Röhrig U.F., Guidoni L., Rothlisberger U.
ISSN
0006-2960 (Print)
ISSN-L
0006-2960
Statut éditorial
Publié
Date de publication
2002
Peer-reviewed
Oui
Volume
41
Numéro
35
Pages
10799-10809
Langue
anglais
Résumé
We present molecular dynamics simulations of bovine rhodopsin in a membrane mimetic environment based on the recently refined X-ray structure of the pigment. The interactions between the protonated Schiff base and the protein moiety are explored both with the chromophore in the dark-adapted 11-cis and in the photoisomerized all-trans form. Comparison of simulations with Glu181 in different protonation states strongly suggests that this loop residue located close to the 11-cis bond bears a negative charge. Restrained molecular dynamics simulations also provide evidence that the protein tightly confines the absolute conformation of the retinal around the C12-C13 bond to a positive helicity. 11-cis to all-trans isomerization leads to an internally strained chromophore, which relaxes after a few nanoseconds by a switching of the ionone ring to an essentially planar all-trans conformation. This structural transition of the retinal induces in turn significant conformational changes of the protein backbone, especially in helix VI. Our results suggest a possible molecular mechanism for the early steps of intramolecular signal transduction in a prototypical G-protein-coupled receptor.
Mots-clé
Animals, Cattle, Computational Biology/methods, Computer Simulation, Crystallography, X-Ray, Glutamic Acid/chemistry, Hydrogen-Ion Concentration, Isomerism, Membrane Proteins/chemistry, Membrane Proteins/physiology, Models, Molecular, Molecular Mimicry, Protein Conformation, Protons, Retinaldehyde/chemistry, Retinoids/chemistry, Rhodopsin/chemistry, Rhodopsin/physiology, Signal Transduction, Software, Thermodynamics
Pubmed
Web of science
Création de la notice
30/10/2015 9:56
Dernière modification de la notice
20/08/2019 17:17
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