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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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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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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Classifying the Binding Modes of Disordered Proteins.

Monika Fuxreiter1,2

  • 1Department of Biomedical Sciences, University of Padova, 35131 Padova, Italy.

International Journal of Molecular Sciences
|November 19, 2020
PubMed
Summary
This summary is machine-generated.

Disordered proteins bind partners flexibly. A new classification scheme categorizes these binding modes, including disorder-to-order, disordered, and fuzzy binding, based on conformational changes.

Keywords:
conformational heterogeneitycontext-dependencedisordered proteinfuzzy bindingprotein interaction

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Systems Biology

Background:

  • Intrinsically disordered proteins (IDPs) are crucial interaction hubs in cellular pathways.
  • The coupled folding-to-binding model fails to explain the versatile interactions of IDPs.

Purpose of the Study:

  • To propose a classification scheme for the binding modes of disordered protein regions.
  • To characterize binding based on conformational heterogeneity in the bound state.

Main Methods:

  • Classification of binding modes based on conformational properties of disordered protein regions upon partner binding.
  • Analysis of structural continuum and context-dependent interaction behaviors.

Main Results:

  • Introduced three binding modes: disorder-to-order transitions, disordered binding, and fuzzy binding.
  • Fuzzy binding encompasses variable disorder, polymorphic structures, conditional folding, and dynamic interactions.
  • The scheme captures the structural continuum and context-dependent nature of IDP interactions.

Conclusions:

  • The proposed classification provides a framework for understanding the diverse binding mechanisms of disordered protein regions.
  • This scheme elucidates how conformational heterogeneity contributes to the functional versatility of IDPs.
  • It highlights the importance of considering the dynamic and context-dependent nature of protein-protein interactions involving disordered regions.