Related Experiment Video
Updated: Sep 18, 2025

Real-time In Vitro Monitoring of Odorant Receptor Activation by an Odorant in the Vapor Phase
Published on: April 23, 2019
How allosteric mutations control ligand binding in Lipocalin protein: odorant binding protein as a test case
Maxence Lalis1, Lucie Moitrier2, Miriam Jäger3
1Institut de Chimie de Nice UMR7272, Université Côte d'Azur, CNRS, 28 Avenue Valrose, Nice, 06108, France.
Researchers uncovered how lipocalins, proteins crucial for molecular transport, recognize targets. Key structural regions and allosteric effects were identified, advancing protein design for specific binding applications.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Lipocalins are essential mammalian proteins for binding and transporting diverse molecules.
- The precise mechanisms of target recognition in lipocalins remain largely unknown.
- Odorant-binding proteins (OBPs), a subset of lipocalins, are critical for olfaction and chemical communication.
Purpose of the Study:
- To elucidate the molecular mechanisms governing target recognition in lipocalins.
- To identify specific structural elements responsible for ligand entry and binding pocket interactions.
- To investigate allosteric influences on ligand binding within the lipocalin family.
Main Methods:
- Utilized an integrative approach combining computational numerical modeling.
- Performed experimental validation to confirm computational findings.
- Focused on structural analysis of odorant-binding proteins (OBPs).
Main Results:
- Identified critical structural regions that control molecular entry into the OBP binding pocket.
- Demonstrated that modifications to these regions abolish molecular recognition.
- Discovered that alterations in distant protein regions impact ligand binding, indicating allosteric regulation.
Conclusions:
- Structural regions regulating ligand entry are vital for lipocalin function.
- Allosteric mechanisms play a significant role in lipocalin-ligand interactions.
- Findings provide a foundation for designing lipocalins with tailored binding specificities.
More Related Videos
08:00Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
Published on: October 4, 2024
07:41A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
Related Concept Videos
Cooperative Allosteric Transitions
Ligand Binding and Linkage
Allosteric Regulation
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...