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Updated: Jun 21, 2026
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
The PTB domain: a modular domain with multiple function.
1Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, PO Box 12233, Research Triangle Park, NC 27709, USA. obryan@niehs.nih.gov
Current Opinion in Drug Discovery & Development
|August 4, 2009
Summary
Cellular communication relies on protein complexes, not just linear cascades. Phosphotyrosine binding (PTB) domains are versatile, interacting with diverse ligands beyond phosphorylated proteins, impacting cell signaling.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Cellular communication is crucial for organism function.
- Signal transduction involves complex protein interactions, not just linear cascades.
- Dysregulation of these complexes can lead to diseases like cancer.
Purpose of the Study:
- To explore the multifaceted roles of protein recognition domains in signal transduction.
- To investigate the ligand-binding versatility of phosphotyrosine binding (PTB) domains.
Main Methods:
- Analysis of protein-protein interactions.
- Biochemical assays to determine ligand binding specificity.
- Molecular biology techniques to study complex assembly.
Main Results:
- Signal transduction involves dynamic, multiprotein complex assembly.
- Modular domains like SH2, SH3, and PTB mediate complex formation.
- PTB domains exhibit unexpected flexibility, binding phospholipids and non-phosphorylated proteins.
Conclusions:
- PTB domains are more versatile than previously understood.
- The flexibility of PTB domains allows for broader cellular target interactions.
- Understanding these interactions is key to deciphering cell signaling and disease mechanisms.
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