期刊
CHEMISTRY & BIOLOGY
卷 21, 期 3, 页码 369-378出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2014.01.006
关键词
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资金
- Ministerio de Ciencia e Innovacion (Spain) [SAF2011-30216-C02-01]
- Grups de Recerca Consolidats de la Generalitat de Catalunya [2009 SGR 1402]
- Fundacion Ramon Areces
- CIG grant from the European Commission
- FI-AGAUR Fellowship
- AGAUR
- Instituto de Salud Carlos III
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 entry to the binding pocket of visual receptors to the specific conformation adopted by the receptor and by the molecular architecture defined by specific amino acids in the binding pocket and the retinal entry site, as well as the topology of the retinal analog. Overall, our findings highlight the specificity of the ligand-opsin interactions, a feature that can be shared by other G-protein-coupled receptors.
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