Related Experiment Video
Updated: Nov 11, 2025

10:34
Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
Published on: April 23, 2017
7.1K
An immunologically friendly classification of non-peptidic ligands
Lindy Edwards1, Rebecca Jackson1,2, James A Overton1,2
1Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, 9420 Athena Circle La Jolla, CA 92037, USA.
Database : the Journal of Biological Databases and Curation
|March 27, 2021
Summary
The Immune Epitope Database (IEDB) improved access to non-peptidic epitope data by simplifying its search hierarchy. This enhancement benefits immunologists by making diverse immune epitope information more discoverable.
Area of Science:
- Immunology
- Bioinformatics
- Data Science
Background:
- The Immune Epitope Database (IEDB) is a public resource for experimental immune epitope data.
- Current search functionalities primarily cater to peptidic epitopes, using single-letter codes and NCBI taxonomy.
- Accessing non-peptidic epitope data (carbohydrates, lipids, chemicals, drugs) is challenging due to inconsistent naming and search limitations.
Purpose of the Study:
- To enhance the accessibility of non-peptidic epitope data within the IEDB.
- To simplify the hierarchical structure used for searching non-peptidic epitopes.
- To improve data retrieval for immunologists and researchers studying diverse epitope types.
Main Methods:
- Revising and simplifying the non-peptidic hierarchy in the IEDB search interface.
- Implementing standardized naming conventions for non-peptidic epitopes.
- Evaluating the impact of hierarchy simplification on data searchability.
Main Results:
- Successful simplification of the non-peptidic epitope hierarchy.
- Improved ease of searching and accessing data for non-peptidic epitopes.
- Enhanced user experience for immunologists seeking comprehensive epitope information.
Conclusions:
- The IEDB has successfully improved access to non-peptidic epitope data through a simplified search hierarchy.
- These improvements facilitate broader research by making diverse immune epitope information more readily available.
- The updated IEDB resource supports a more comprehensive understanding of immune responses involving various epitope types.
More Related Videos
Related Concept Videos
Ligand Binding Sites
14.4K
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...
14.4K
Ligand Binding Sites
8.3K
8.3K
Ligand-gated Ion Channels
13.4K
Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
13.4K
Ligand Binding and Linkage
3.7K
3.7K
Ligand Binding and Linkage
5.2K
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...
5.2K
Metal-Ligand Bonds
22.7K
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
22.7K

