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Related Concept Videos

Antibody Structure01:10

Antibody Structure

66.0K
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...
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Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Antibody Structure and Classes01:25

Antibody Structure and Classes

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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.
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Updated: Feb 23, 2026

Selection of Transporter-Targeted Inhibitory Nanobodies by Solid-Supported-Membrane SSM-Based Electrophysiology
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A Unified Dataset for Antibody and Nanobody Design Including Sequence, Structure, and Binding Affinity Data.

Yikai Wu1, Xuejiao Liu2, Karin Hrovatin3

  • 1Human Phenome Institute, Fudan University, Shanghai, China.

Scientific Data
|February 21, 2026
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Summary

We created the Antibody and Nanobody Design Dataset (ANDD), integrating diverse data for antibody and nanobody design. This unified resource advances deep generative models for improved therapeutic and diagnostic applications.

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Area of Science:

  • Biotechnology
  • Computational Biology
  • Immunology

Background:

  • Deep generative models show promise for antibody and nanobody design.
  • Existing datasets are fragmented and inconsistent, limiting model training.
  • There is a need for a unified, comprehensive dataset for antibody and nanobody research.

Purpose of the Study:

  • To introduce the Antibody and Nanobody Design Dataset (ANDD).
  • To create a unified resource integrating sequence, structure, antigen, and affinity data.
  • To facilitate the training of deep generative models for antibody and nanobody design.

Main Methods:

  • Integrated data from 15 diverse sources into a single dataset.
  • Included antibody/nanobody sequences, structural data, and antigen sequences.
  • Augmented affinity data using the ANTIPASTI model for binding affinity prediction.

Main Results:

  • ANDD comprises 48,683 antibody/nanobody sequences and 24,941 structural entries.
  • The dataset contains 12,575 antigen sequences and 9,557 affinity values.
  • ANDD is the largest dataset for antibody/nanobody-antigen pairs with affinity data.

Conclusions:

  • ANDD addresses data fragmentation and inconsistency challenges.
  • The dataset provides a robust foundation for training deep generative models.
  • ANDD enables better modeling of antibody/nanobody-antigen interactions for novel therapeutic development.