ArticleStructure (London, England : 1993)2015
The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Bioinspired Dynamic Remodeling of Excited-State Pathways for High-Performance Stimuli-Responsive Materials.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Structural analysis of rhodopsin states in megabody complexes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A short story on how chromophore is hydrolyzed from rhodopsin for recycling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- FRET sensors reveal the retinal entry pathway in the G protein-coupled receptor rhodopsin.iScience · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021Review
- Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization.Journal of visualized experiments : JoVE · 2020Article
- A benchmark study of loop modeling methods applied to G protein-coupled receptors.Journal of computer-aided molecular design · 2019Article
- In Silico Studies Targeting G-protein Coupled Receptors for Drug Research Against Parkinson's Disease.Current neuropharmacology · 2018Article
- 7×7 RMSD matrix: A new method for quantitative comparison of the transmembrane domain structures in the G-protein coupled receptors.Journal of structural biology · 2017Article
- G Protein-Coupled Receptors Contain Two Conserved Packing Clusters.Biophysical journal · 2017Article
- What Do Structures Tell Us About Chemokine Receptor Function and Antagonism?Annual review of biophysics · 2017Review
- Article
- Structural basis of ligand interaction with atypical chemokine receptor 3.Nature communications · 2017Article
- G protein-coupled receptors: the evolution of structural insight.AIMS biophysics · 2017Article
- Gonadotropin-Releasing Hormone (GnRH) Receptor Structure and GnRH Binding.Frontiers in endocrinology · 2017Review
- Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work.Frontiers in endocrinology · 2017Review
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Rhodopsin, a light-activated G protein coupled receptor (GPCR), has been the subject of numerous biochemical and structural investigations, serving as a model receptor for GPCRs and their activation. We present the 2.3-Å resolution structure of native source rhodopsin stabilized in a conformation competent for G protein binding. An extensive water-mediated hydrogen bond network linking the chromophore binding site to the site of G protein binding is observed, providing connections to conserved motifs essential for GPCR activation. Comparison of this extensive solvent-mediated hydrogen-bonding network with the positions of ordered solvent in earlier crystallographic structures of rhodopsin photointermediates reveals both static structural and dynamic functional water-protein interactions present during the activation process. When considered along with observations that solvent occupies similar positions in the structures of other GPCRs, these analyses strongly support an integral role for this dynamic ordered water network in both rhodopsin and GPCR activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.