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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Inducible Operons: lac Operon01:25

Inducible Operons: lac Operon

The lac operon in Escherichia coli is a model for understanding inducible gene regulation and metabolic flexibility. It integrates local control by lactose and global regulation through catabolite repression, enabling E. coli to preferentially metabolize glucose when available and switch to lactose utilization when glucose is scarce.Structure and Function of the lac OperonThe lac operon contains three structural genes: lacZ (β-galactosidase), lacY (lactose permease), and lacA (thiogalactoside...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
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Published on: May 17, 2024

Lactose binding to galectin-1 modulates structural dynamics, increases conformational entropy, and occurs with

Irina V Nesmelova1, Elena Ermakova, Vladimir A Daragan

  • 1Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

Journal of Molecular Biology
|February 27, 2010
PubMed
Summary

Galectin-1 (gal-1) undergoes structural changes upon lactose binding, with dynamic loops folding around the sugar. This protein-carbohydrate interaction exhibits negative cooperativity, influencing gal-1

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Galectins, including galectin-1 (gal-1), are lectins that bind beta-galactosides.
  • Gal-1 plays roles in cell adhesion, migration, and tumor angiogenesis by interacting with cell surface glycoconjugates.

Purpose of the Study:

  • To investigate lactose binding to galectin-1 (gal-1) using biophysical techniques.
  • To determine the solution NMR structures of gal-1 in both lactose-bound and unbound states.
  • To elucidate the structural dynamics and binding mechanisms of gal-1-carbohydrate interactions.

Main Methods:

  • Heteronuclear NMR spectroscopy to derive solution structures and analyze binding.
  • Molecular modeling and dynamics simulations to study protein flexibility and signal transmission.
  • Circular Dichroism (CD) spectroscopy to assess structural changes.
  • Isothermal Titration Calorimetry (ITC) to quantify binding thermodynamics.

Main Results:

  • Lactose binding induces conformational changes in gal-1, with loops folding around the bound molecule and altering protein dynamics.
  • Gal-1 exhibits negative cooperativity in lactose binding, with the first lactose molecule binding more strongly than the second.
  • NMR and molecular dynamics data suggest that ligand binding at one site influences the other binding site through structural communication.

Conclusions:

  • Lactose binding to galectin-1 involves significant structural rearrangements and dynamic alterations, contributing to binding free energy.
  • The negative cooperativity observed in gal-1-lactose binding provides insights into the regulation of lectin function.
  • This study enhances understanding of galectin structure-function relationships and general principles of protein-carbohydrate recognition.