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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Updated: May 21, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
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Published on: May 14, 2021

Intermolecular β-sheet Formation Guides the Interaction between Ubiquitin-like Modifier FAT10 and Adapter Protein

Charlotte Weiss1, Sarah Overall2, Nicola Catone3

  • 1Department of Chemistry, University of Konstanz, Konstanz 78464, Germany.

Journal of the American Chemical Society
|May 20, 2026
PubMed
Summary
This summary is machine-generated.

The ubiquitin-like modifier FAT10 targets proteins for degradation. The adapter protein NUB1L stabilizes FAT10 in an unfolded state, crucial for inflammation-linked proteostasis and protein degradation.

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Published on: March 14, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The ubiquitin-like modifier FAT10 targets proteins for degradation by the 26S proteasome under inflammatory conditions.
  • The intrinsically disordered nature of FAT10 and its interaction with adapter protein NUB1L are implicated in substrate degradation.

Purpose of the Study:

  • To investigate the N-domain of FAT10 and its interaction with NUB1L using magic-angle spinning (MAS) NMR spectroscopy.
  • To elucidate the structural changes in FAT10 upon binding to NUB1L and their functional implications.

Main Methods:

  • Magic-angle spinning (MAS) NMR spectroscopy was employed to study the N-domain of FAT10.
  • Analysis of the structural dynamics and intermolecular interactions between FAT10 and NUB1L.

Main Results:

  • Binding to NUB1L induces structural changes in the intrinsically disordered N-domain of FAT10.
  • A disordered region of FAT10 becomes structured upon NUB1L binding, forming a loop and an intermolecular β-sheet.
  • NUB1L acts as a holdase, stabilizing FAT10 in an unfolded state essential for proteasomal degradation.

Conclusions:

  • NUB1L stabilizes FAT10 in an unfolded conformation, facilitating its degradation by the proteasome.
  • FAT10's ability to interact in both folded and unfolded states is critical for its function in inflammation-linked proteostasis.