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Binding specificity of retinal analogs to photoactivated visual pigments suggest mechanism for fine-tuning GPCR-ligand interactions

Autor
Srinivasan, S.; Ramon, E.; Cordomi, A.; Garriga, P.
Tipus d'activitat
Article en revista
Revista
Chemistry and biology
Data de publicació
2014-03-20
Volum
21
Número
3
Pàgina inicial
369
Pàgina final
378
DOI
https://doi.org/10.1016/j.chembiol.2014.01.006 Obrir en finestra nova
Projecte finançador
ALTERACIONES PROCESOS ACTIVACION Y TRANSDUCCION DE SEÑAL DE RECEPTORES ACOPLADOS A PROTEINAS G
GRUP DE BIOTECNOLOGIA MOL.LECULAR I INDUSTRIAL
URL
http://www.sciencedirect.com/science/article/pii/S1074552114000295 Obrir en finestra nova
Resum
11-cis-retinal acts as an inverse agonist stabilizing the inactive conformation of visual pigments, and upon photoactivation, it isomerizes to all-trans-retinal, initiating signal transduction. We have analyzed opsin regeneration with retinal analogs for rhodopsin and red cone opsin. We find differential binding of the analogs to the receptors after photobleaching and a dependence of the binding kinetics on the oligomerization state of the protein. The results outline the sensitivity of retinal ...
Paraules clau
Protein-coupled Receptor, Crystal-structure, Fluorescence Spectroscopy, Crystallographic Analysis, Conformational Stability, Squid Rhodopsin, Molecular-basis, 9-methyl Group, Covalent Bond, Opsin Mutants
Grup de recerca
CEBIM - Centre de Biotecnologia Molecular
GBMI - Grup de Biotecnologia Molecular i Industrial

Participants