ArticleBiochemistry2014
Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Histamine-modulated wettability switching in G-protein-coupled receptor inspired nanochannel for potential drug screening and biosensing.Nature communications · 2025Article
- Hidden water's influence on rhodopsin activation.Biophysical journal · 2024Review
- Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time.ACS central science · 2023Article
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.Nature communications · 2021Article
- Artificial Photosynthesis: Is Computation Ready for the Challenge Ahead?Nanomaterials (Basel, Switzerland) · 2021Review
- Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins.The Journal of membrane biology · 2019Review
- Insights into the function of opioid receptors from molecular dynamics simulations of available crystal structures.British journal of pharmacology · 2018Review
- Lipids Alter Rhodopsin Function via Ligand-like and Solvent-like Interactions.Biophysical journal · 2018Article
- Signaling within Allosteric Machines: Signal Transmission Pathways Inside G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2017Review
- Molecular Dynamics Methodologies for Probing Cannabinoid Ligand/Receptor Interaction.Methods in enzymology · 2017Article
- Vibrational resonance, allostery, and activation in rhodopsin-like G protein-coupled receptors.Scientific reports · 2016Article
- Quasi-elastic Neutron Scattering Reveals Ligand-Induced Protein Dynamics of a G-Protein-Coupled Receptor.The journal of physical chemistry letters · 2016Article
- Ultraslow Water-Mediated Transmembrane Interactions Regulate the Activation of A2A Adenosine Receptor.Biophysical journal · 2016Article
- Photosynthetic diode: electron transport rectification by wetting the quinone cofactor.Physical chemistry chemical physics : PCCP · 2015Article
- Retinal Conformation Changes Rhodopsin's Dynamic Ensemble.Biophysical journal · 2015Article
- Retinal Flip in Rhodopsin Activation?Biophysical journal · 2015Article
- Retinal Flips the Script.Biophysical journal · 2015Article
- Quantifying conformational changes in GPCRs: glimpse of a common functional mechanism.BMC bioinformatics · 2015Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Rhodopsin, the mammalian dim-light receptor, is one of the best-characterized G-protein-coupled receptors, a pharmaceutically important class of membrane proteins that has garnered a great deal of attention because of the recent availability of structural information. Yet the mechanism of rhodopsin activation is not fully understood. Here, we use microsecond-scale all-atom molecular dynamics simulations, validated by solid-state (2)H nuclear magnetic resonance spectroscopy, to understand the transition between the dark and metarhodopsin I (Meta I) states. Our analysis of these simulations reveals striking differences in ligand flexibility between the two states. Retinal is much more dynamic in Meta I, adopting an elongated conformation similar to that seen in the recent activelike crystal structures. Surprisingly, this elongation corresponds to both a dramatic influx of bulk water into the hydrophobic core of the protein and a concerted transition in the highly conserved Trp265(6.48) residue. In addition, enhanced ligand flexibility upon light activation provides an explanation for the different retinal orientations observed in X-ray crystal structures of active rhodopsin.
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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.