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Related Concept Videos

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.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Protein topology and allostery.

Juan Xie1, Luhua Lai2

  • 1Center for Quantitative Biology, Peking University, Beijing 100871, China.

Current Opinion in Structural Biology
|February 18, 2020
PubMed
Summary

Allosteric regulation, crucial for biological processes, depends on protein structure. Researchers explored preferred protein folds and allosteric site locations, aiding in designing novel allosteric proteins.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology

Background:

  • Allostery is vital in biological processes, yet the number of identified allosteric proteins remains limited.
  • Understanding the relationship between protein topology and allosteric regulation is essential.
  • The preferred protein folds and common locations of allosteric sites require further investigation.

Purpose of the Study:

  • To investigate how protein topology influences allosteric regulation.
  • To identify preferred protein folds in allosteric proteins.
  • To characterize the typical locations of allosteric sites in different protein types.

Main Methods:

  • Analysis of known allosteric proteins and their structures.
  • Comparison of allosteric protein folds with general protein fold distributions.
  • Mapping of allosteric and orthosteric site locations within protein structures.

Main Results:

  • Allosteric sites are frequently located between chains or domains in multi-component proteins.
  • In single-domain proteins, allosteric sites often reside opposite the orthosteric site.
  • The immunoglobulin-like fold is underrepresented among allosteric proteins, while others like alpha-beta plaits and specific domains (PDZ, WW) are common.

Conclusions:

  • Protein topology significantly impacts allosteric regulation mechanisms.
  • Specific protein folds and domain architectures are favored for allosteric function.
  • Insights gained facilitate the rational design of novel allosteric proteins and materials.