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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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...
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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...
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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...
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Designed allosteric protein logic.

Tjaša Plaper1, Estera Merljak1, Tina Fink1

  • 1Department of Synthetic Biology and Immunology, National Institute of Chemistry, Hajdrihova 19, SI-1000, Ljubljana, Slovenia.

Cell Discovery
|January 16, 2024
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Summary
This summary is machine-generated.

Researchers developed INSRTR, a novel protein regulation system. This method precisely controls protein function, enabling new biotechnological and therapeutic applications by inserting peptides into target proteins.

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Area of Science:

  • Molecular Biology
  • Biotechnology
  • Protein Engineering

Background:

  • Protein function regulation is crucial for biological processes.
  • Controlling specific protein activity offers valuable tools for research and medicine.

Purpose of the Study:

  • To introduce a versatile and robust protein regulation system named INSRTR.
  • To demonstrate INSRTR's ability to control protein function for diverse applications.

Main Methods:

  • Developed INSRTR by inserting regulatory peptides into target protein loops.
  • Utilized coiled-coil interactions for protein function inactivation or activation.
  • Employed a machine learning model to predict optimal insertion sites.
  • Tested INSRTR on various proteins including enzymes, signaling mediators, and antibody domains.

Main Results:

  • INSRTR demonstrated versatility across diverse protein folds and functions.
  • Achieved precise control over protein activity, including inactivation and activation.
  • Successfully implemented two-input logic functions with rapid response in mammalian cells.
  • Showcased INSRTR's robustness in engineered T cells for chimeric antigen receptor therapy.

Conclusions:

  • INSRTR is a powerful and generally applicable tool for precise protein function control.
  • This strategy advances understanding of biological processes.
  • INSRTR holds significant potential for biotechnological and therapeutic interventions.