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Related Concept Videos

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
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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

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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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Related Experiment Video

Updated: May 20, 2026

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
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The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

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Multiple binding partners.

Norbert W Seidler1

  • 1Department of Biochemistry, Kansas City University of Medicine and Biosciences, Kansas City, MO, USA.

Advances in Experimental Medicine and Biology
|August 2, 2012
PubMed
Summary
This summary is machine-generated.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts with many proteins, revealing common structural features and potential roles in neurodegenerative diseases. This research maps the GAPDH interactome, highlighting its involvement in cellular stress responses.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme with known diverse cellular functions beyond its canonical role.
  • Understanding the full spectrum of GAPDH interactions is crucial for elucidating its multifaceted cellular roles.

Purpose of the Study:

  • To present the interactome of GAPDH, categorizing binding partners by function and structure.
  • To identify common structural motifs and consensus sequences in GAPDH-interacting proteins and polynucleotides.
  • To explore the potential involvement of GAPDH in age-related neurodegenerative diseases.

Main Methods:

  • Systematic identification and categorization of GAPDH interacting proteins.
  • Bioinformatic analysis to identify common structural features and consensus sequences.
  • Review of recent discoveries linking GAPDH-associated proteins to neurodegenerative conditions.

Main Results:

  • The GAPDH interactome reveals common structural features, including acidic dipeptide sequences in binding partners.
  • Consensus sequences for target polynucleotides interacting with GAPDH have been identified.
  • Proteins associated with age-related neurodegenerative diseases are frequently found to bind GAPDH, suggesting a role in these conditions.

Conclusions:

  • GAPDH interactome analysis provides insights into its structural and functional network.
  • GAPDH may function as a global sensor for cellular conformational stress, particularly in aging and neurodegeneration.
  • GAPDH exhibits diverse enzymatic activities beyond oxidoreductase, including peroxidase, nitrosylase, mono-ADP-ribosylase, and kinase functions.