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Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Protein Networks02:26

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,...
Protein Organization01:24

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.
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

BEID: database for sequence-structure-function information on antigen-antibody interactions.

Joo Chuan Tong1, Chun Meng Song, Paul Thiam Joo Tan

  • 1Institute for Infocomm Research, 1 Fusionopolis Way, #21-01 Connexis, South Tower, Singapore. jctong@i2r.a-star.edu.sg

Bioinformation
|February 25, 2009
PubMed
Summary
This summary is machine-generated.

The B-cell Epitope Interaction Database (BEID) provides detailed Ig-antigen interaction data. This resource aids in understanding molecular recognition and developing B-cell epitope predictors.

Keywords:
antibodyantigendatabaseepitopesequence-structure function

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Area of Science:

  • Immunology
  • Structural Biology
  • Bioinformatics

Background:

  • Immunoglobulin (Ig)-antigen interactions are crucial for adaptive immunity.
  • Understanding these interactions at a molecular level is essential for vaccine design and therapeutic development.
  • Existing databases may lack comprehensive sequence-structure-function data for Ig-antigen complexes.

Purpose of the Study:

  • To present the B-cell Epitope Interaction Database (BEID) as a curated, open-access resource.
  • To detail the scope and content of the current BEID version, including Ig-antigen complexes.
  • To highlight the database's utility for studying molecular recognition and computational epitope prediction.

Main Methods:

  • Data extraction and curation from the Protein Data Bank (PDB).
  • Manual verification, classification, and analysis of intermolecular interactions within Ig-antigen complexes.
  • Inclusion of detailed interaction parameters like solvent accessibility, hydrogen bonds, and interface area.

Main Results:

  • The BEID database currently contains 164 antigens, 126 Ig, and 189 Ig-antigen complexes.
  • Each entry is manually verified and analyzed for specific intermolecular interaction features.
  • The database offers a user-friendly search tool and downloadable schematic diagrams.

Conclusions:

  • BEID serves as a valuable, comprehensive resource for Ig-antigen interaction data.
  • The database enhances understanding of the molecular basis of B-cell recognition.
  • BEID is a critical data source for advancing computational B-cell epitope prediction tools.