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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...
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...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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 pathway,...

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Related Experiment Video

Updated: Jun 24, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Allosteric switches: remote controls for proteins.

Thorsten Berg1

  • 1Department of Molecular Biology, Max Planck Institute of Biochemistry and Cluster for Integrated Protein Science Munich, Am Klopferspitz 18, 82152 Martinsried, Germany. berg@biochem.mpg.de

Angewandte Chemie (International Ed. in English)
|March 13, 2009
PubMed
Summary
This summary is machine-generated.

Developing a universal protein activity switch is challenging. This study explores an adaptable protein switch strategy to indirectly control protein function, offering a simpler alternative to small-molecule modulators.

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Area of Science:

  • Molecular Biology
  • Protein Engineering
  • Biochemistry

Background:

  • Developing selective small-molecule modulators for all human protein domains is complex.
  • Targeting protein function often requires specific inhibitors or activators for each protein.

Purpose of the Study:

  • To investigate the feasibility of using an adaptable protein switch for indirect protein activity control.
  • To explore an alternative strategy to traditional small-molecule drug discovery for protein modulation.

Main Methods:

  • Protein engineering of a versatile switch module.
  • Fusion of the switch module to target proteins.
  • Assays to measure modulated protein activity.

Main Results:

  • Demonstration of indirect control over protein function via the engineered switch.
  • Potential for broad applicability across different protein types.

Conclusions:

  • An adaptable protein switch system offers a promising alternative for modulating protein activity.
  • This approach could simplify the development of tools for studying and manipulating protein function.