Evidence map›Paper›PMID 18463093›Full record

ArticleThe Journal of biological chemistry2008

Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region.

Tatsuro Shimamura, Kenji Hiraki, Naoko Takahashi, Tetsuya Hori, Hideo Ago, Katsuyoshi Masuda, Koji Takio, Masaji Ishiguro, Masashi Miyano

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
9.5field-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

61 citing papers in PubMed, 133 citations in OpenAlex.

  1. G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024
    Article
  2. Article
  3. Review
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  5. Article
  6. Review
  7. Improved homology modeling of the human & rat EPBMC molecular and cell biology · 2019
    Article
  8. Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  16. The leukotriene BBiochemistry and biophysics reports · 2015
    Article
  17. Review
  18. Review
  19. Review
  20. Article

1 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

9 authors at 2 institutions in 1 country.

Tatsuro ShimamuraRIKEN SPring-8 Center, Harima Institute, Kouto, Sayo, Hyogo, Japan.
Kenji Hiraki
Naoko Takahashi
Tetsuya Hori
Hideo Ago
Katsuyoshi Masuda
Koji Takio
Masaji Ishiguro
Masashi Miyano
SPring-8 · JPSuntory Foundation for Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-protein-coupled receptors play a key step in cellular signal transduction cascades by transducing various extracellular signals via G-proteins. Rhodopsin is a prototypical G-protein-coupled receptor involved in the retinal visual signaling cascade. We determined the structure of squid rhodopsin at 3.7A resolution, which transduces signals through the G(q) protein to the phosphoinositol cascade. The structure showed seven transmembrane helices and an amphipathic helix H8 has similar geometry to structures from bovine rhodopsin, coupling to G(t), and human beta(2)-adrenergic receptor, coupling to G(s). Notably, squid rhodopsin contains a well structured cytoplasmic region involved in the interaction with G-proteins, and this region is flexible or disordered in bovine rhodopsin and human beta(2)-adrenergic receptor. The transmembrane helices 5 and 6 are longer and extrude into the cytoplasm. The distal C-terminal tail contains a short hydrophilic alpha-helix CH after the palmitoylated cysteine residues. The residues in the distal C-terminal tail interact with the neighboring residues in the second cytoplasmic loop, the extruded transmembrane helices 5 and 6, and the short helix H8. Additionally, the Tyr-111, Asn-87, and Asn-185 residues are located within hydrogen-bonding distances from the nitrogen atom of the Schiff base.

Indexed as

Amino Acid SequenceAnimalsCattleCrystallography, X-RayCytoplasmDecapodiformesHydrogen BondingMolecular Sequence DataProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Adrenergic, beta-2Receptors, G-Protein-CoupledRhodopsinSequence Homology, Amino AcidReceptors, Adrenergic, beta-2Receptors, G-Protein-CoupledRhodopsin

Identifiers

PMID18463093
PMCPMC2440622
OpenAlexW2056884349

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.