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

Sundaramoorthy Srinivasan, Eva Ramon, Arnau Cordomí, Pere Garriga

Research output: Contribution to journalArticleResearchpeer-review

14 Citations (Scopus)

Abstract

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. © 2014 Elsevier Ltd.
Original languageEnglish
Pages (from-to)369-378
JournalChemistry and Biology
Volume21
Issue number3
DOIs
Publication statusPublished - 20 Mar 2014

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