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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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions.

Peter Tompa1, Monika Fuxreiter

  • 1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary. tompa@enzim.hu

Trends in Biochemical Sciences
|December 7, 2007
PubMed
Summary

Protein complexes exhibit structural disorder, termed "fuzziness," which is crucial for their function. This phenomenon, encompassing static to dynamic and segmental to full disorder, is key to understanding protein interactions and regulation.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Current research focuses on static macromolecular interactions to determine protein function.
  • Protein complexes are increasingly recognized to exhibit structural disorder and polymorphism.
  • This structural variability has been largely overlooked in previous studies.

Purpose of the Study:

  • To introduce and define a new term, 'fuzziness,' for structural disorder in protein complexes.
  • To classify the different types of protein complex disorder.
  • To highlight the importance of disorder in protein function and regulation.

Main Methods:

  • Literature review and synthesis of existing findings on protein complex structures.
  • Conceptual framework development for classifying structural disorder.
  • Analysis of the implications of disorder for protein-protein interactions.

Main Results:

  • Structural disorder in protein complexes can be categorized into four mechanistic types.
  • These types represent a spectrum from static to dynamic and segmental to full disorder.
  • The term 'fuzziness' is proposed to encompass this widespread phenomenon.

Conclusions:

  • 'Fuzziness' is a general and important characteristic of protein complexes.
  • Understanding protein disorder is essential for comprehending the interactome.
  • This concept will be integral to future research on protein interactions and regulation.