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Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Related Experiment Video

Updated: Jul 16, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Conformational changes in mannan-binding lectin bound to ligand surfaces.

Mingdong Dong¹, Sailong Xu, Cristiano L P Oliveira

¹Interdisciplinary Nanoscience Center (iNANO), Department of Physiucs and Astronomy, University of Aarhus, Aarhus C, Denmark.

Journal of Immunology (Baltimore, Md. : 1950)

|February 22, 2007

Summary

Mannan-binding lectin (MBL) in solution has a stable, ramified structure. Upon binding to surfaces, MBL undergoes significant conformational changes, stretching to expose its ligand-binding domains, revealing crucial immune recognition mechanics.

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Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

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Published on: May 17, 2024

Area of Science:

Structural biology
Immunology
Biophysics

Background:

Soluble protein binding to surfaces is crucial for immune response initiation.
Structural details of protein-surface interactions in immunity remain largely unknown.
Mannan-binding lectin (MBL) is a key pattern recognition molecule in innate immunity.

Purpose of the Study:

To elucidate the structural dynamics of MBL in solution and upon surface binding.
To provide insight into the molecular mechanisms of MBL-mediated immune recognition.
To investigate the role of surface topography in protein conformational changes.

Main Methods:

Small-angle X-ray scattering (SAXS) for solution structure analysis.
High-resolution atomic force microscopy (AFM) for single-molecule surface interaction studies.
Analysis of MBL quaternary structure transitions.

Main Results:

MBL in solution adopts a stable, ramified structure with rotational symmetry.
Surface-immobilized ligands induce a significant structural transition in MBL.
MBL transitions to a stretched state, separating its ligand-binding domains upon surface interaction.

Conclusions:

MBL exhibits large conformational changes in quaternary structure upon surface binding.
The transition from soluble to surface-bound states is influenced by surface topography.
These findings offer direct evidence for the role of mechanical changes in MBL-mediated immune recognition.