Related Experiment Video
Updated: Jul 9, 2026

09:39
Mapping Dysfunctional Protein-Protein Interactions in Disease
Published on: October 24, 2025
PPIDD: an extraction and visualisation method of biological protein-protein interfaces
Vincent Benoit1, Marie-Hélène Mucchielli-Giorgi, Benoît Dumont
1Centre de Génétique Moléculaire, UPR2167, Gif/Orsay DNA MicroArray Platform, F-91198 Gif-sur-Yvette, France.
Biochimie
|December 19, 2007
Summary
A new database, PPIDD (Protein-Protein Interface Description Database), distinguishes specific biological protein-protein interactions from non-specific crystal contacts in PDB structures. This tool aids in understanding protein assembly determinants.
Area of Science:
- Structural Biology
- Bioinformatics
- Computational Biology
Background:
- Protein-protein complex data is crucial but not readily available from PDB structures.
- Distinguishing specific biological interfaces from non-specific crystallographic contacts is challenging.
- Existing databases lack the ability to differentiate between biological and crystallographic interfaces.
Purpose of the Study:
- To develop an innovative tool for extracting and visualizing biological protein-protein interfaces.
- To focus on well-identified classes of protein assemblies and their interfaces.
- To facilitate the construction of interface subsets for understanding interaction determinants.
Main Methods:
- Development of the Protein-Protein Interface Description Database (PPIDD).
- Extraction and visualization of biological interfaces from annotated crystallographic structures.
- Representation and export of protein assemblies and interfaces in an extended PDBML format.
Main Results:
- PPIDD successfully extracts and visualizes biological protein-protein interfaces.
- The tool allows representation and export of protein assemblies and their interfaces.
- PPIDD enables the creation of custom interface subsets based on user-defined characteristics.
Conclusions:
- PPIDD provides a novel solution for accessing reliable protein-protein complex datasets.
- The database aids in distinguishing specific biological interactions from non-specific ones.
- PPIDD enhances the understanding of determinants driving specific protein-protein interactions.
More Related Videos
Related Concept Videos
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...
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...
Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
Ligand Binding Sites
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

