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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

62.7K
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-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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Ligand Binding and Linkage00:49

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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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Ligand Binding and Linkage00:49

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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Related Experiment Video

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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
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Correlation Between Allosteric and Orthosteric Sites.

Weilin Zhang1,2, Juan Xie1,2, Luhua Lai3,4

  • 1College of Chemistry and Molecular Engineering, Peking University, Beijing, China.

Advances in Experimental Medicine and Biology
|November 11, 2019
PubMed
Summary

Understanding allosteric and orthosteric site correlation reveals information transmission in allosteric regulation. This knowledge aids in developing new allosteric drugs by studying ligand binding and mutations.

Keywords:
Community analysisCorrelationElastic network modelEvolutionary analysisMolecular dynamicsMutual informationRigid-body simulationStatistical coupling analysisTwo state Go̅ model

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Area of Science:

  • Biochemistry and Molecular Biology
  • Pharmacology
  • Computational Biology

Background:

  • Allosteric and orthosteric sites are crucial for protein function and regulation.
  • Understanding the correlation between these sites is key to deciphering biological information transfer.
  • This correlation is vital for the development of targeted allosteric drugs.

Purpose of the Study:

  • To provide an overview of correlation studies between allosteric and orthosteric sites.
  • To highlight recent advancements in evolutionary and simulation-based dynamic studies.
  • To discuss future research directions in allosteric regulation.

Main Methods:

  • Review of existing literature on allosteric-orthosteric site correlations.
  • Analysis of evolutionary studies on protein dynamics.
  • Examination of simulation-based dynamic studies.

Main Results:

  • Perturbations at allosteric sites influence orthosteric sites through various mechanisms.
  • Evolutionary and dynamic studies provide insights into the transmission of information.
  • Current research offers a foundation for novel allosteric drug discovery strategies.

Conclusions:

  • The correlation between allosteric and orthosteric sites is a fundamental aspect of biological regulation.
  • Advanced computational and evolutionary methods are powerful tools for studying these interactions.
  • Further research holds significant promise for the future of allosteric drug development.