ArticleBiophysical journal2017
G Protein-Coupled Receptors Contain Two Conserved Packing Clusters.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
14 citing papers in PubMed.
- An RFamide signaling system balances turning and forward locomotion to optimize global food search inJournal of biosciences · 2025Article
- Neuroprotective Effects of a Serotonin Receptor Peptide Following ShamEndocrinology, diabetes and metabolism journal · 2023Article
- Modeling the Orthosteric Binding Site of the G Protein-Coupled Odorant Receptor OR5K1.Journal of chemical information and modeling · 2023Article
- Protons taken hostage: Dynamic H-bond networks of the pH-sensing GPR68.Computational and structural biotechnology journal · 2023Article
- Is there a common allosteric binding site for G-protein coupled receptors?Journal of computer-aided molecular design · 2022Article
- Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- The Many Faces of G Protein-Coupled Receptor 143, an Atypical Intracellular Receptor.Frontiers in molecular biosciences · 2022Review
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Deconstructing the transmembrane core of class A G protein-coupled receptors.Trends in biochemical sciences · 2021Review
- Polyphenols and Visual Health: Potential Effects on Degenerative Retinal Diseases.Molecules (Basel, Switzerland) · 2021Review
- A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin.Structure (London, England : 1993) · 2020Article
- Structural instability and divergence from conserved residues underlie intracellular retention of mammalian odorant receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanism of Hormone Peptide Activation of a GPCR: Angiotensin II Activated State of ATJournal of chemical information and modeling · 2019Article
- The molecular and cellular basis of rhodopsin retinitis pigmentosa reveals potential strategies for therapy.Progress in retinal and eye research · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
G protein-coupled receptors (GPCRs) have evolved a seven-transmembrane helix framework that is responsive to a wide range of extracellular signals. An analysis of the interior packing of family A GPCR crystal structures reveals two clusters of highly packed residues that facilitate tight transmembrane helix association. These clusters are centered on amino acid positions 2.47 and 4.53, which are highly conserved as alanine and serine, respectively. Ala2.47 mediates the interaction between helices H1 and H2, while Ser4.53 mediates the interaction between helices H3 and H4. The helical interfaces outside of these clusters are lined with residues that are more loosely packed, a structural feature that facilitates motion of helices H5, H6, and H7, which is required for receptor activation. Mutation of the conserved small side chain at position 4.53 within packing cluster 2 is shown to disrupt the structure of the visual receptor rhodopsin, whereas sites in packing cluster 1 (e.g., positions 1.46 and 2.47) are more tolerant to mutation but affect the overall stability of the protein. These findings reveal a common structural scaffold of GPCRs that is important for receptor folding and activation.
Indexed as
Identifiers
What OpenQuestion holds
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.