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Related Concept Videos

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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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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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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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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Designing Silk-silk Protein Alloy Materials for Biomedical Applications
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Supertertiary protein structure affects an allosteric network.

Louise Laursen1, Johanna Kliche1, Stefano Gianni2,3

  • 1Department of Medical Biochemistry and Microbiology, Uppsala University, SE-75123 Uppsala, Sweden.

Proceedings of the National Academy of Sciences of the United States of America
|September 15, 2020
PubMed
Summary
This summary is machine-generated.

Protein allosteric networks are significantly influenced by their surrounding protein structures. Understanding these supertertiary structures is key to predicting protein allostery and function.

Keywords:
allosterydouble-mutant cyclekineticsprotein interactionssupertertiary structure

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Area of Science:

  • Structural biology
  • Biochemistry
  • Protein dynamics

Background:

  • Allosteric regulation is crucial for protein function, often involving structural changes.
  • PDZ domains are commonly studied for allostery but yield conflicting results.
  • The impact of protein supramodular structures on allosteric networks remains unclear.

Purpose of the Study:

  • To experimentally map the allosteric network within a PDZ:ligand complex.
  • To investigate how supertertiary structures influence these allosteric networks.
  • To determine the generalizability of structure-dependent allostery in proteins.

Main Methods:

  • Experimental mapping of allosteric networks.
  • Comparative analysis of PDZ:ligand complexes in isolation versus within supramodular structures.

Main Results:

  • Allosteric networks in PDZ domains are highly sensitive to the supertertiary context.
  • The presence of adjacent protein domains significantly alters allosteric network properties.
  • Allosteric network behavior is not solely determined by isolated domain structure.

Conclusions:

  • Supertertiary structure is a critical determinant of protein allosteric networks.
  • Allosteric network sensitivity to adjacent domains is likely a common feature of supramodular proteins.
  • Findings impact predictions of allosteric regulation and quantitative descriptions of allostery.