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Related Concept Videos

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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 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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Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
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The Equilibrium Binding Constant and Binding Strength02:18

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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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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Explaining and Predicting Allostery with Allosteric Database and Modern Analytical Techniques.

Jinyin Zha1, Mingyu Li1, Ren Kong2

  • 1Shanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine at Shanghai, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

Journal of Molecular Biology
|February 8, 2022
PubMed
Summary
This summary is machine-generated.

The Allosteric Database (ASD) provides crucial data for studying allostery, a key biological process. This review highlights how ASD facilitates discoveries in drug targets and allosteric modulators.

Keywords:
allosteric drugallosteric mechanismallosteric sitemachine learningprotein sequence

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Bioinformatics

Background:

  • Allostery regulates protein activity via non-functional site binding, crucial for biological processes and therapeutic interventions.
  • Studying allostery is challenging due to limited available data.
  • The Allosteric Database (ASD) was established to address this knowledge gap by compiling extensive allosteric data.

Purpose of the Study:

  • To review the four data categories within the Allosteric Database (ASD).
  • To examine how researchers utilize ASD data for various studies.
  • To summarize discoveries of novel drug targets and allosteric modulators enabled by ASD.

Main Methods:

  • Categorization of allosteric data within the ASD.
  • Review of research methodologies employing ASD data.
  • Analysis of research topics, analytical approaches, and findings derived from ASD.

Main Results:

  • ASD encompasses four distinct categories of allosteric data.
  • Researchers have successfully applied ASD data to investigate diverse research questions.
  • The database has contributed to identifying new drug targets and developing allosteric modulators.

Conclusions:

  • ASD serves as a valuable resource for allosteric research.
  • This review demonstrates the utility of ASD in advancing drug discovery and understanding allosteric mechanisms.
  • The findings aim to inspire novel applications and further research utilizing ASD data.