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Updated: Dec 30, 2025

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
Published on: December 1, 2020
Protein Interaction Domains: Structural Features and Drug Discovery Applications (Part 2)
Marian Vincenzi1, Flavia Anna Mercurio1, Marilisa Leone1
1Institute of Biostructures and Bioimaging, National Research Council (CNR), Via Mezzocannone 16, 80134 Naples, Italy.
Protein Interaction Domains (PIDs) are key to cellular signaling and disease pathways. This review explores PIDs that bind standard peptides, highlighting their therapeutic potential and challenges in drug development.
Area of Science:
- Molecular Biology
- Structural Biology
- Drug Discovery
Background:
- Proteins utilize domains for modular organization and interaction recruitment.
- Protein Interaction Domains (PIDs) are critical for signal transduction and physiological/disease pathways.
- Targeting PIDs offers a therapeutic strategy for modulating interaction networks.
Purpose of the Study:
- To review PIDs that recognize post-translationally modified peptide segments.
- To examine PIDs interacting with standard amino acid peptide sequences.
- To consolidate structural and interactome information on PIDs.
Main Methods:
- Comprehensive database searches (PDB, Pfam, SMART) for structural and interactome data.
- Literature review using PubMed to identify recent research on PIDs.
- Analysis of domain subfamilies and their interaction partners.
Main Results:
- PIDs exhibit diverse structural features and recognize various consensus sequences.
- PIDs are implicated in disease onset and progression, including cancer and viral infections.
- PIDs have potential applications in personalized medicine.
Conclusions:
- PIDs are versatile and play significant roles in health and disease.
- While peptide/peptidomimetic inhibitors are being developed, further optimization for drug-likeness and affinity is required.
- Targeting PIDs remains a promising avenue for novel therapeutic development.
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