Related Experiment Video
Updated: Aug 19, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
Published on: August 1, 2017
Structural classification of CDR-H3 in antibodies
H Shirai1, A Kidera, H Nakamura
1Department of Bioinformatics, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
Insights
The antibody heavy chain's third complementarity determining region (CDR-H3) shows sequence-structure rules. These findings aid in antibody structural modeling and design.
Area of Science:
- Immunology
- Structural Biology
- Biochemistry
Background:
- The third complementarity determining region of the antibody heavy chain (CDR-H3) exhibits significant sequence and length variability.
- Unlike other CDRs, CDR-H3 lacks established canonical structures, complicating sequence-structure relationship predictions.
Purpose of the Study:
- To investigate and define rules governing the conformational dependence of CDR-H3 on its amino acid sequence.
- To provide a basis for improved antibody structural modeling and design.
Main Methods:
- Analysis of 55 CDR-H3 segments from experimentally determined crystal structures.
- Derivation of sequence-based rules for CDR-H3 conformation.
Main Results:
- Several key rules were identified that partly explain CDR-H3 conformation based on amino acid sequence.
- The derived rules are physically plausible and offer insights into CDR-H3 structural determinants.
Conclusions:
- The established rules offer a significant advancement in understanding CDR-H3 structure-sequence relationships.
- These findings are expected to be valuable for the rational design and modeling of antibodies.
Abstract:
Large varieties in the lengths and the amino acid sequences of the third complementarity determining region of the antibody heavy chain (CDR-H3) have made it difficult to establish a relationship between the sequences and the tertiary structures, in contrast to the other CDRs, which are classified by their canonical structures. A total of 55 CDR-H3 segments from well determined crystal structures were analyzed, and we have derived several remarkable rules, which could partly govern the CDR-H3 conformation dependence on the sequence. Since the rules are physically reasonable, they are expected to be applicable to structural modeling and design of antibodies.
More Related Videos
07:26High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
Published on: July 18, 2017
11:17Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Related Concept Videos
Antibody Structure
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...
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Naming Enantiomers
Prochirality
Structure of Cadherins