Evidence map›Paper›PMID 25584517›Full record

ArticleNature communications2015

Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors.

Thomas A Hopf, Satoshi Morinaga, Sayoko Ihara, Kazushige Touhara, Debora S Marks, Richard Benton

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
8.0field-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

63 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular bases of insect odorant receptor function: specificity and evolution.Biological reviews of the Cambridge Philosophical Society · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Structure modelling of odorant receptor fromComputational and structural biotechnology journal · 2023
    Article
  13. Proceedings. Biological sciences · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

3 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

6 authors at 3 institutions in 3 countries.

Thomas A Hopf1] Department of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115, USA [2] Department of Informatics, Technische Universität München, 85748 Garching, Germany.
Satoshi Morinaga1] Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan [2] ERATO Touhara Chemosensory Signal Project, JST, The University of Tokyo, Tokyo 113-8657, Japan.
Sayoko Ihara1] Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan [2] ERATO Touhara Chemosensory Signal Project, JST, The University of Tokyo, Tokyo 113-8657, Japan.
Kazushige Touhara1] Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan [2] ERATO Touhara Chemosensory Signal Project, JST, The University of Tokyo, Tokyo 113-8657, Japan.
Debora S MarksDepartment of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Richard BentonCenter for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, CH-1015 Lausanne, Switzerland.
The University of Tokyo · JPHarvard University · USUniversity of Lausanne · CH

Funding

Accelerated Determination of 3D Structures of Proteins and ComplexesR01GM106303 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI SANDER, CHRIS · 2013 to 2016
$1.7M
European Research Council 205202European Research Council 615094NIGMS NIH HHS R01 GM106303
6 · The paper itself

Abstract

Insect odorant receptors (ORs) comprise an enormous protein family that translates environmental chemical signals into neuronal electrical activity. These heptahelical receptors are proposed to function as ligand-gated ion channels and/or to act metabotropically as G protein-coupled receptors (GPCRs). Resolving their signalling mechanism has been hampered by the lack of tertiary structural information and primary sequence similarity to other proteins. We use amino acid evolutionary covariation across these ORs to define restraints on structural proximity of residue pairs, which permit de novo generation of three-dimensional models. The validity of our analysis is supported by the location of functionally important residues in highly constrained regions of the protein. Importantly, insect OR models exhibit a distinct transmembrane domain packing arrangement to that of canonical GPCRs, establishing the structural unrelatedness of these receptor families. The evolutionary couplings and models predict odour binding and ion conduction domains, and provide a template for rationale structure-activity dissection.

Indexed as

Evolution, MolecularAmino AcidsAnimalsInsectaReceptors, OdorantXenopusAmino AcidsReceptors, Odorant

Identifiers

PMID25584517
PMCPMC4364406
OpenAlexW2111064199

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.