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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

DisProt: the Database of Disordered Proteins.

Megan Sickmeier1, Justin A Hamilton, Tanguy LeGall

  • 1Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, IN 46202, USA.

Nucleic Acids Research
|December 6, 2006
PubMed
Summary

Intrinsically disordered proteins (IDPs) lack fixed structures but perform crucial regulatory and signaling functions. The DisProt database organizes experimental data on IDPs, aiding research and bioinformatics studies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Intrinsically disordered proteins (IDPs) lack stable three-dimensional structures under physiological conditions.
  • Despite lacking fixed structures, IDPs are vital for biological regulation, signaling, and control.
  • Protein intrinsic disorder facilitates unique interaction patterns, including high-specificity low-affinity binding.

Purpose of the Study:

  • To establish the DisProt database, a centralized resource for intrinsically disordered proteins (IDPs).
  • To link structural disorder information with functional roles of IDPs.
  • To facilitate bioinformatics studies related to protein disorder.

Main Methods:

  • Curating and organizing experimentally determined information on protein disorder.
  • Compiling data on the functional associations of intrinsically disordered proteins.
  • Making the DisProt database publicly accessible online.

Main Results:

  • DisProt provides a comprehensive collection of knowledge on the experimental characterization of IDPs.
  • The database links protein disorder to specific biological functions and interaction mechanisms.
  • DisProt serves as a valuable resource for advancing IDP research.

Conclusions:

  • The DisProt database addresses the need for organized information on intrinsically disordered proteins.
  • DisProt enhances the study of protein disorder by integrating structural and functional data.
  • This resource supports diverse bioinformatics analyses and promotes a deeper understanding of IDP functions.