Antibodies (immunoglobulins) are Y-shaped proteins produced by B cells to neutralize pathogens. They consist of two heavy chains and two light chains, forming a structure with variable regions (paratopes) that bind antigens with high specificity .
Antigen-antibody binding involves weak, non-covalent interactions (e.g., hydrogen bonds, van der Waals forces) between epitopes (antigen regions) and paratopes . Key properties:
Specificity: Governed by hypervariable complementarity-determining regions (CDRs) .
Affinity maturation: Somatic hypermutation improves binding strength by 10- to 100-fold .
Cross-reactivity: Occurs when antibodies bind structurally similar epitopes, contributing to autoimmune conditions .
Function: Maps residue-level interactions (hydrogen bonds, salt bridges) across 403+ complexes .
Applications: Benchmarking epitope prediction algorithms and antibody humanization .
Diverse antibody repertoires (>10¹¹ specificities) arise through:
Interface prediction: Machine learning models trained on 4,638 Ab-Ag structures struggle with hydrophobic/hydrogen bond balance .
Nanotechnology integration: Antibody-conjugated nanoparticles show promise in targeted drug delivery and MRI contrast enhancement .
Error rates: ~15% of PDB antigen-antibody entries require manual correction in AACDB .
| Field | Antibody Use Case | Example |
|---|---|---|
| Diagnostics | ELISA, lateral flow assays | HIV detection via gp120 binding |
| Therapeutics | Monoclonal antibodies (e.g., trastuzumab) | HER2-positive breast cancer |
| Vaccine Design | Epitope mapping for synthetic vaccines | SARS-CoV-2 spike protein targets |