ArticleNature structural & molecular biology2016
Free backbone carbonyls mediate rhodopsin activation.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Mapping signal transduction in bistable jumping spider rhodopsin 1.Biophysical journal · 2026Article
- Coordination of bilayer properties by an inward-rectifier KJournal of structural biology: X · 2024Article
- Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study.Journal of biomolecular NMR · 2023Article
- Cholesterol Biases the Conformational Landscape of the Chemokine Receptor CCR3: A MAS SSNMR-Filtered Molecular Dynamics Study.Journal of chemical information and modeling · 2023Article
- Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- Deconstructing the transmembrane core of class A G protein-coupled receptors.Trends in biochemical sciences · 2021Review
- A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin.Structure (London, England : 1993) · 2020Article
- Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.Biochimica et biophysica acta. General subjects · 2018Review
- Protein Sequence and Membrane Lipid Roles in the Activation Kinetics of Bovine and Human Rhodopsins.Biophysical journal · 2017Article
- G Protein-Coupled Receptors Contain Two Conserved Packing Clusters.Biophysical journal · 2017Article
- Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin.Proceedings. Biological sciences · 2017Article
- Retinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation.Nature communications · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Conserved prolines in the transmembrane helices of G-protein-coupled receptors (GPCRs) are often considered to function as hinges that divide the helix into two segments capable of independent motion. Depending on their potential to hydrogen-bond, the free C=O groups associated with these prolines can facilitate conformational flexibility, conformational switching or stabilization of the receptor structure. To address the role of conserved prolines in family A GPCRs through solid-state NMR spectroscopy, we focus on bovine rhodopsin, a GPCR in the visual receptor subfamily. The free backbone C=O groups on helices H5 and H7 stabilize the inactive rhodopsin structure through hydrogen-bonds to residues on adjacent helices. In response to light-induced isomerization of the retinal chromophore, hydrogen-bonding interactions involving these C=O groups are released, thus facilitating repacking of H5 and H7 onto the transmembrane core of the receptor. These results provide insights into the multiple structural and functional roles of prolines in membrane proteins.
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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.