Evidence map›Paper›PMID 19182802›Full record

ArticleNature structural & molecular biology2009

Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation.

Shivani Ahuja, Viktor Hornak, Elsa C Y Yan, Natalie Syrett, Joseph A Goncalves, Amiram Hirshfeld, Martine Ziliox, Thomas P Sakmar, Mordechai Sheves, Philip J Reeves and 2 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
14.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

123 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 · 2025
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  6. Coordination of bilayer properties by an inward-rectifier KJournal of structural biology: X · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020
    Review
  20. Review

63 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 3 countries.

Shivani AhujaDepartment of Physics and Astronomy, Stony Brook University, Stony Brook, New York 11794-5215, USA.
Viktor Hornak
Elsa C Y Yan
Natalie Syrett
Joseph A Goncalves
Amiram Hirshfeld
Martine Ziliox
Thomas P Sakmar
Mordechai Sheves
Philip J Reeves
Steven O Smith
Markus Eilers
Stony Brook University · USUniversity of Essex · GBWeizmann Institute of Science · ILRockefeller University · USYale University · US

Funding

Structure and Activation Mechanism of the Visual Pigment RhodopsinR01GM041412 · NIGMS · YALE UNIVERSITY · PI SMITH, STEVEN OWEN · 1989 to 2014
$4.4M
600 MHZ SOLID STATE NMR SPECTROMETERS10RR013889 · NCRR · STATE UNIVERSITY NEW YORK STONY BROOK · PI SMITH, STEVEN OWEN · 1999 to 1999
–
NCRR NIH HHS S10 RR13889NIGMS NIH HHS GM-41412NIGMS NIH HHS R01 GM041412
6 · The paper itself

Abstract

The second extracellular loop (EL2) of rhodopsin forms a cap over the binding site of its photoreactive 11-cis retinylidene chromophore. A crucial question has been whether EL2 forms a reversible gate that opens upon activation or acts as a rigid barrier. Distance measurements using solid-state (13)C NMR spectroscopy between the retinal chromophore and the beta4 strand of EL2 show that the loop is displaced from the retinal binding site upon activation, and there is a rearrangement in the hydrogen-bonding networks connecting EL2 with the extracellular ends of transmembrane helices H4, H5 and H6. NMR measurements further reveal that structural changes in EL2 are coupled to the motion of helix H5 and breaking of the ionic lock that regulates activation. These results provide a comprehensive view of how retinal isomerization triggers helix motion and activation in this prototypical G protein-coupled receptor.

Indexed as

AnimalsCattleCell LineHumansLightModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingRetinaldehydeRhodopsinRetinaldehydeRhodopsin

Identifiers

PMID19182802
PMCPMC2705779
OpenAlexW2104155178

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.