Evidence map›Paper›PMID 40549142›Full record

ArticleCellular and molecular life sciences : CMLS2025

How allosteric mutations control ligand binding in Lipocalin protein: odorant binding protein as a test case.

Maxence Lalis, Lucie Moitrier, Miriam Jäger, Cornelia Meinert, Marine Brulé, Christine Belloir, Nykola C Jones, Søren V Hoffmann, Sébastien Fiorucci, Steffen Wolf and 2 more

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Beyond olfaction: New insights into human odorant binding proteins.Protein science : a publication of the Protein Society · 2026
    Review
  2. 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

12 authors.

Maxence Lalis *Institut de Chimie de Nice UMR7272, Université Côte d'Azur, CNRS, 28 Avenue Valrose, Nice, 06108, France.
Lucie Moitrier *Centre des Sciences du Goût et de l'Alimentation, Institut Agro, CNRS, INRAE, Université de Bourgogne, Dijon, F-21000, France.
Miriam JägerBiomolecular Dynamics, Institute of Physics, University of Freiburg, 79111, Freiburg, Germany.
Cornelia MeinertInstitut de Chimie de Nice UMR7272, Université Côte d'Azur, CNRS, 28 Avenue Valrose, Nice, 06108, France.
Marine BruléCentre des Sciences du Goût et de l'Alimentation, Institut Agro, CNRS, INRAE, Université de Bourgogne, Dijon, F-21000, France.
Christine BelloirCentre des Sciences du Goût et de l'Alimentation, Institut Agro, CNRS, INRAE, Université de Bourgogne, Dijon, F-21000, France.
Nykola C JonesDepartment of Physics and Astronomy, Aarhus University, Aarhus, 8000, Denmark.
Søren V HoffmannDepartment of Physics and Astronomy, Aarhus University, Aarhus, 8000, Denmark.
Sébastien FiorucciInstitut de Chimie de Nice UMR7272, Université Côte d'Azur, CNRS, 28 Avenue Valrose, Nice, 06108, France.
Steffen WolfBiomolecular Dynamics, Institute of Physics, University of Freiburg, 79111, Freiburg, Germany.
Loïc BriandCentre des Sciences du Goût et de l'Alimentation, Institut Agro, CNRS, INRAE, Université de Bourgogne, Dijon, F-21000, France. loic.briand@inrae.fr.
Jérémie TopinInstitut de Chimie de Nice UMR7272, Université Côte d'Azur, CNRS, 28 Avenue Valrose, Nice, 06108, France. jeremie.topin@univ-cotedazur.fr.ORCID http://orcid.org/0000-0003-1470-1206

Funding

Agence Nationale de la Recherche ANR-15-IDEX-01Deutsche Forschungsgemeinschaft WO 2410/2-1H2020 Research Infrastructures No 101004806
6 · The paper itself

Abstract

Lipocalins are a family of proteins found in mammals that are essential for the binding and transport of various molecules, but the mechanisms underlying their target recognition are still unclear. To answer this question, we studied odorant-binding proteins (OBPs), a specific type of lipocalin involved in chemical communication and olfaction. Using an integrative approach combining numerical modelling and experimental validation, we identified key structural regions that regulate the entry of molecules into the binding pocket. Modification of these regions disrupts molecular recognition, highlighting their importance for function. In addition, we found that changes in distant parts of the protein influence binding, shedding light on allosteric mechanisms. These results advance our understanding of lipocalin function and open up avenues for the design of proteins with targeted binding properties.

Indexed as

LipocalinsMutationReceptors, OdorantAllosteric RegulationAnimalsBinding SitesHumansLigandsModels, MolecularProtein BindingLigandsLipocalinsodorant-binding proteinReceptors, OdorantCircular dichroismIsothermal titration calorimetryLipocalinMolecular dynamicsOdorant binding proteinSite-directed mutagenesis

Identifiers

PMID40549142
PMCPMC12185845

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.