Antibody CDR Loops Fingerprint
Monoclonal Antibody (Rituximab) of CD20
- The general structure of all antibodies is very similar
- It is composed of one constant and one variable domain from each heavy and light chain of the antibody
- The loops at the tip are referred to as the complementarily determining regions (CDRs)
- The CDR loops are extremely variable, allowing millions of antibodies with slightly different tip structures, as antigen binding sites
- Rituximab is a widely used monoclonal antibody drug for treating certain lymphomasand autoimmune diseases. It is a chimeric monoclonal antibody against the protein CD20, which is primarily found on the surface of B cells.
- There are two protein structure data (3BKY and 2OSL) available in PDB
- Fingerprint comparison for CDR loops of monoclonal antibody (Rituximab) is show below table.
Antigen-Antibody Recognition & Binding: Rituximab Fab fragment in complex with an epitope peptide of the large extra-cellular loop (residues 163–187) of CD20.
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More Applications |
| Objective | Application |
|---|---|
| Reveal the nature of protein folding variations | |
| Mutation vs. change in folding conformation | |
| Antibody (Rituximab) of CD20 fingerprint | |
| Antibody optimization by fingerprint | |
| Design peptide for a specific folding conformation | |
| Comparison of protein conformations | |
| Expose similarity and dissimilarity for conformers | |
| Comparison between Insulin Receptor and IGF-1 Receptor | |
| Misfolding in Amyloid Beta-42 | |
| Similarity score for conformation search | |
| ATP Binding Sites on Kinases | |
| Predict multiple protein targets for drug |