Evidence map›Paper›PMID 23904486›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins.

Erin L Devine, Daniel D Oprian, Douglas L Theobald

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. The Origins of GPCRs.International journal of molecular sciences · 2026
    Review
  2. Structural Mechanism of an Efficacy Photoswitch Targeting the βAngewandte Chemie (International ed. in English) · 2026
    Article
  3. Graph-Based Deep Learning Models for Predicting pJournal of chemical information and modeling · 2026
    Article
  4. Article
  5. Article
  6. Molecular advances to study the function, evolution and spectral tuning of arthropod visual opsins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Retinoids and Retinal Diseases.Annual review of vision science · 2016
    Review
  18. Article
  19. Molecular bases for the selection of the chromophore of animal rhodopsins.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

Erin L DevineDepartment of Biochemistry, Brandeis University, Waltham, MA 02454, USA.
Daniel D Oprian
Douglas L Theobald
Brandeis University · US

Funding

STRUCTURE/FUNCTION STUDIES OF RHODOPSINR01EY007965 · NEI · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1989 to 2017
$6.2M
Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
Evolution of enzyme structure and function viewed at atomic resolutionR01GM096053 · NIGMS · BRANDEIS UNIVERSITY · PI Douglas Lowell Theobald · 2011 to 2026
$3.6M
Bayesian analysis of structural shape and conformationR01GM094468 · NIGMS · BRANDEIS UNIVERSITY · PI THEOBALD, DOUGLAS LOWELL · 2010 to 2014
$1.4M
NEI NIH HHS EY007965NEI NIH HHS R01 EY007965NIGMS NIH HHS 5T32GM007596NIGMS NIH HHS GM094468NIGMS NIH HHS GM096053NIGMS NIH HHS R01 GM094468NIGMS NIH HHS R01 GM096053NIGMS NIH HHS T32 GM007596
6 · The paper itself

Abstract

Type I and type II rhodopsins share several structural features including a G protein-coupled receptor fold and a highly conserved active-site Lys residue in the seventh transmembrane segment of the protein. However, the two families lack significant sequence similarity that would indicate common ancestry. Consequently, the rhodopsin fold and conserved Lys are widely thought to have arisen from functional constraints during convergent evolution. To test for the existence of such a constraint, we asked whether it were possible to relocate the highly conserved Lys296 in the visual pigment bovine rhodopsin. We show here that the Lys can be moved to three other locations in the protein while maintaining the ability to form a pigment with 11-cis-retinal and activate the G protein transducin in a light-dependent manner. These results contradict the convergent hypothesis and support the homology of type I and type II rhodopsins by divergent evolution from a common ancestral protein.

Indexed as

Evolution, MolecularModels, MolecularProtein ConformationAnimalsCatalytic DomainCattleEye ProteinsLysineModels, BiologicalRhodopsinSpectrophotometry, UltravioletTransducinEye ProteinsLysineRhodopsinTransducin

Identifiers

PMID23904486
PMCPMC3746867
OpenAlexW2026661045

What OpenQuestion holds

Textmetadata
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.