Evidence map›Paper›PMID 12697900›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding.

Valerie Campanacci, Audrey Lartigue, B Martin Hällberg, T Alwyn Jones, Marie-Thèrese Giudici-Orticoni, Mariella Tegoni, Christian Cambillau

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

57 citing papers in PubMed, 155 citations in OpenAlex.

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  14. Chemosensory protein 4 is required forFrontiers in physiology · 2022
    Article
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  20. Molecular Modeling of Chemosensory Protein 3 fromInternational journal of molecular sciences · 2020
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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

7 authors at 3 institutions in 2 countries.

Valerie CampanacciArchitecture et Fonction des Macromolécules Biologiques, Unité Mixte de Recherche 6098, Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I & II, 31 Chemin J. Aiguier, 13402 Marseille Cedex 20, France.
Audrey Lartigue
B Martin Hällberg
T Alwyn Jones
Marie-Thèrese Giudici-Orticoni
Mariella Tegoni
Christian Cambillau
Uppsala University · SEArchitecture et Fonction des Macromolécules Biologiques · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chemosensory proteins (CSPs) have been proposed to transport hydrophobic chemicals from air to olfactory or taste receptors. They have been isolated from several sensory organs of a wide range of insect species. The x-ray structure of CSPMbraA6, a 112-aa antennal protein from the moth Mamestra brassicae (Mbra), was shown to exhibit a novel type of alpha-helical fold. We have performed a structural and binding study of CSPMbraA6 to get some insights into its possible molecular function. Tryptophan fluorescence quenching demonstrates the ability of CSPMbraA6 to bind several types of semio-chemicals or surrogate ligands with microM K(d). Its crystal structure in complex with one of these compounds, 12-bromo-dodecanol, reveals extensive conformational changes on binding, resulting in the formation of a large cavity filled by three ligand molecules. Furthermore, binding cooperativity was demonstrated for some ligands, suggesting a stepwise binding. The peculiar rearrangement of CSPMbraA6 conformation and the cooperativity phenomenon might trigger the recognition of chemicals by receptors and induce subsequent signal transduction.

Indexed as

AnimalsInsect ProteinsLigandsModels, MolecularMothsMutagenesis, Site-DirectedProtein BindingProtein ConformationSpectrometry, FluorescenceTryptophanCSPMbraA6 protein, Mamestra brassicaeInsect ProteinsLigandsTryptophan

Identifiers

PMID12697900
PMCPMC154299
OpenAlexW2018882399

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.