Related Experiment Video
Updated: Mar 2, 2026

09:37
An Integrated Approach for Microprotein Identification and Sequence Analysis
Published on: July 12, 2022
4.0K
GenProBiS: web server for mapping of sequence variants to protein binding sites
Janez Konc1,2, Blaz Skrlj1, Nika Erzen1
1National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Nucleic Acids Research
|May 13, 2017
Summary
The GenProBiS web server maps genetic variants to protein structures and binding sites, aiding drug discovery and medical research. It helps identify potentially harmful mutations within protein interaction regions.
Area of Science:
- Biochemistry
- Bioinformatics
- Structural Biology
Background:
- Identifying deleterious sequence variants is crucial for advancing human and veterinary medicine and drug discovery.
- Understanding variant impact requires mapping them to protein structures and functional sites.
- Existing tools may lack comprehensive mapping to diverse protein binding interactions.
Purpose of the Study:
- To introduce the GenProBiS web server for mapping sequence variants to protein structures and binding sites.
- To provide a tool for exploring variants in relation to protein-protein, protein-nucleic acid, protein-compound, and protein-metal ion interactions.
- To facilitate hypothesis generation in medicine and drug discovery by visualizing variant locations within functional regions.
Main Methods:
- Utilized the Protein Binding Sites (ProBiS) algorithm for local structural comparisons to define binding sites.
- Employed the ProBiS-ligands approach for ligand transposition to identify binding sites on query proteins.
- Generated 3D grids representing binding site surfaces and integrated with WebGL for visualization.
- Mapped human somatic mutations and non-synonymous single nucleotide polymorphisms from 21 species to approximately 80,000 Protein Data Bank (PDB) structures.
Main Results:
- The GenProBiS server successfully maps sequence variants to various protein binding sites, including post-translational modification sites.
- It provides intuitive visual exploration of variants, such as cancer-related mutations, within predicted binding regions.
- The server integrates data from ~80,000 PDB structures, offering broad applicability.
Conclusions:
- GenProBiS offers a valuable resource for researchers by linking genetic variants to specific functional regions on protein structures.
- The tool enhances the discovery of potentially deleterious variants and supports hypothesis generation in biomedical research.
- The web server is freely accessible, promoting wider use in medicine and drug discovery.
Related Concept Videos
Conserved Binding Sites
5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Conserved Binding Sites
2.0K
2.0K
Ligand Binding and Linkage
5.7K
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...
5.7K
Protein Networks
4.6K
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,...
4.6K
Protein Networks
2.9K
2.9K
Protein-protein Interfaces
14.9K
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...
14.9K

