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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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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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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 Proteins-ATCase01:19

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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...
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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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Simulations of allosteric transitions.

Ron Elber1

  • 1Department of Chemistry and Biochemistry, Institute of Computational Engineering and Sciences, 1 University Station, ICES, C0200, The University of Texas at Austin, Austin, TX 78712, USA. ron@ices.utexas.edu

Current Opinion in Structural Biology
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Summary

This review explores how proteins transmit signals over large distances. It examines theoretical and computational methods for understanding how small effector binding events trigger massive protein shape changes.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Allosteric transitions fine-tune protein activity through effector binding.
  • Effector binding initiates large conformational changes involving domain motions.

Purpose of the Study:

  • To investigate the mechanisms of signal propagation in allosteric transitions.
  • To understand how small perturbations are amplified to induce large-scale protein conformational changes.
  • To explore the focus, coherence, and efficiency of signal transmission over long distances.

Main Methods:

  • Review of theoretical approaches.
  • Examination of computational modeling techniques.

Main Results:

  • Allosteric transitions involve complex signal propagation from effector binding sites.
  • Protein conformational changes can be massive, involving thousands of atoms.
  • Signal transmission over large distances in a noisy molecular environment is a key challenge.

Conclusions:

  • Understanding allosteric signal transmission is crucial for deciphering protein regulation.
  • Theoretical and computational methods offer insights into these complex molecular mechanisms.