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Allosteric Regulation01:08

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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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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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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Allosteric Dynamic Control of Binding.

Fidan Sumbul1, Saliha Ece Acuner-Ozbabacan1, Turkan Haliloglu1

  • 1Department of Chemical Engineering and Polymer Research Center, Bogazici University, Istanbul, Turkey.

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|September 5, 2015
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Summary
This summary is machine-generated.

Allosteric mutations are linked to protein hinge positions, influencing binding affinity. This study reveals how these mutations alter protein dynamics and interactions, impacting function.

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Area of Science:

  • Protein dynamics and structural biology
  • Biophysics and computational biology
  • Molecular interactions and allostery

Background:

  • Proteins exhibit dynamic conformational changes crucial for their binding behavior and function.
  • Understanding the relationship between protein dynamics and binding affinity is key to deciphering functional mechanisms.

Purpose of the Study:

  • To investigate the association between allosteric mutations and protein hinge dynamics.
  • To elucidate the mechanism by which mutations at hinge regions allosterically modulate protein binding interactions.

Main Methods:

  • Large-scale statistical analysis of mutation data from the SKEMPI database.
  • Mechanistic studies on human growth hormone (hGH) and pyrin domain (PYD).

Main Results:

  • A significant association was found between allosteric mutations, high-binding-affinity changes, and hinge positions of global protein dynamics.
  • Mutations at hinge regions were shown to allosterically affect binding-site dynamics and induce alternative binding modes.
  • Long-range effects of local perturbations on global dynamics were identified as a mechanism for allosteric modulation.

Conclusions:

  • Protein structural dynamics are critically coupled to the modulation of protein interactions.
  • Allosteric dynamics can be restored through the long-range dissemination of perturbations impacting global dynamics.
  • Findings provide insights into the functional consequences of mutations affecting protein interactions.