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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...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Ligand interaction scan: a general method for engineering ligand-sensitive protein alleles.

Oran Erster1, Miriam Eisenstein, Mordechai Liscovitch

  • 1Department of Biological Regulation, Weizmann Institute of Science, P.O. Box 26, Rehovot 76100, Israel.

Nature Methods
|April 24, 2007
PubMed
Summary

The ligand interaction scan (LIScan) method engineers small molecule-regulated proteins. This chemical-genetic approach uses peptide inserts and ligands for protein function control and drug-target validation.

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Area of Science:

  • Protein engineering
  • Chemical genetics
  • Drug discovery

Background:

  • Protein regulation is crucial for biological processes.
  • Existing methods for drug-target validation have limitations.
  • Engineering controllable protein function is a key challenge.

Purpose of the Study:

  • To introduce a novel method, ligand interaction scan (LIScan), for engineering small molecule-regulated proteins.
  • To provide a complementary approach to existing reverse genetic and chemical-genetic methods.
  • To demonstrate the utility of LIScan for drug-target validation.

Main Methods:

  • Utilized insertional mutagenesis to create a chemical-genetic 'switch'.
  • Incorporated a genetically encoded peptide module with high affinity for a small-molecule ligand.
  • Applied the LIScan method to TEM-1 beta-lactamase using a tetracysteine hexapeptide insert and a biarsenical fluorescein ligand (FlAsH).

Main Results:

  • Successfully engineered a small molecule-regulated protein using the LIScan method.
  • Demonstrated the feasibility of using a peptide module and small molecule ligand for protein control.
  • Validated the LIScan approach with a model protein system (TEM-1 beta-lactamase).

Conclusions:

  • The LIScan method offers a versatile platform for engineering ligand-regulated proteins.
  • This technique provides a valuable tool for drug-target validation and protein engineering.
  • LIScan complements existing chemical-genetic strategies for functional genomics.