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Related Concept Videos

Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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...

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Related Experiment Video

Updated: May 7, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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End binding proteins are obligatory dimers.

Indrani Sen1, Dmitry Veprintsev, Anna Akhmanova

  • 1Laboratory of Biomolecular Research, Paul Scherrer Institut, Villigen PSI, Switzerland.

Plos One
|September 17, 2013
PubMed
Summary
This summary is machine-generated.

End binding (EB) proteins are obligatory dimers, remaining stable at physiological conditions. This finding is crucial for understanding how EB proteins orchestrate dynamic protein networks at growing microtubule ends.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • End binding (EB) proteins are key regulators of microtubule dynamics.
  • They recruit numerous microtubule plus-end tracking proteins (+TIPs) to growing microtubule ends.
  • EB proteins possess an N-terminal calponin homology domain for microtubule tracking and a C-terminal coiled-coil domain for dimerization and partner binding.

Purpose of the Study:

  • To determine the oligomerization state of EB1 and EB3 proteins at physiologically and experimentally relevant concentrations.
  • To assess the stability of EB dimers under varying conditions.
  • To provide mechanistic insights into EB protein function in dynamic microtubule networks.

Main Methods:

  • Multi-angle light scattering (MALS).
  • Fluorescence analytical ultracentrifugation (AUC).

Main Results:

  • EB1 and EB3 proteins form stable dimers.
  • These dimers do not dissociate even at very low nanomolar concentrations.
  • EB dimers remain stable at both room temperature and 37°C.

Conclusions:

  • End binding proteins are obligatory dimers.
  • This dimerization is a prerequisite for +TIP binding and essential for their function.
  • Understanding EB dimerization is critical for modeling EB-dependent dynamic +TIP networks.