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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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...
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...
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...
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...

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Related Experiment Video

Updated: Jun 8, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Ligand dimerization programmed by hybridization to study multimeric ligand-receptor interactions.

Katarzyna Gorska1, Julien Beyrath, Sylvie Fournel

  • 1Institut de Science et Ingenierie Supramoleculaires (ISIS), Université de Strasbourg-CNRS (UMR 7006), 8 allee Gaspard Monge, 67000 Strasbourg, France.

Chemical Communications (Cambridge, England)
|September 21, 2010
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel method to control peptide macrocycle assembly using peptide nucleic acid (PNA) tags. This approach programs ligand-receptor interactions, exemplified by targeting the DR5 receptor involved in TRAIL cytokine signaling.

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Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
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Last Updated: Jun 8, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
09:18

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Chemical Biology

Background:

  • Receptor oligomerization, driven by polyvalent ligands, is crucial for cellular recognition and signal transduction pathways.
  • Understanding and controlling these oligomerization processes are key to modulating cellular responses.

Purpose of the Study:

  • To present a versatile strategy for encoding peptide macrocycles with peptide nucleic acid (PNA) tags.
  • To demonstrate the programming of macrocycle oligomerization via DNA hybridization.
  • To exemplify this approach using a ligand designed to bind the oligomeric Death Receptor 5 (DR5).

Main Methods:

  • Synthesis of peptide macrocycles functionalized with PNA oligomers.
  • Utilizing complementary DNA hybridization to induce or stabilize specific macrocycle oligomeric states.
  • Assessing ligand binding to the DR5 receptor and its modulation by programmed oligomerization.

Main Results:

  • Successfully encoded peptide macrocycles with PNA tags, enabling programmable self-assembly.
  • Demonstrated control over macrocycle oligomerization through hybridization of PNA tags.
  • Showcased the application in creating a ligand that targets the oligomeric DR5 receptor.

Conclusions:

  • The developed PNA-tagging strategy offers a generalizable method for programming the assembly of complex molecular architectures.
  • This approach provides a powerful tool for controlling multivalent ligand-receptor interactions and signaling.
  • The findings have implications for designing targeted therapeutics and understanding biological recognition processes.