The diversity of H 3 loops determines the antigen‐binding tendencies of antibody CDR loops
Open accessAbstract
Of the complementarity-determining regions (CDRs) of antibodies, H3 loops, with varying amino acid sequences and loop lengths, adopt particularly diverse loop conformations. The diversity of H3 conformations produces an array of antigen recognition patterns involving all the CDRs, in which the residue positions actually in contact with the antigen vary considerably. Therefore, for a deeper understanding of antigen recognition, it is necessary to relate the sequence and structural properties of each residue position in each CDR loop to its ability to bind antigens. In this study, we proposed a new method for characterizing the structural features of the CDR loops and obtained the antigen-binding ability of each residue position in each CDR loop. This analysis led to a simple set of rules for identifying probable antigen-binding residues. We also found that the diversity of H3 loop lengths and conformations affects the antigen-binding tendencies of all the CDR loops.
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CDRH3 is very important for antigen recognition.
“CDRH3 possesses the highest sequence and structural diversity of the six CDRs [33] and is very important for antigen recognition [34, 35].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [34]
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- Authors
- Tsuchiya, Y., & Mizuguchi, K.
- Affiliations
- National Institute of Biomedical Innovation, Health and Nutrition (JP)
- Corresponding author
- Tsuchiya, Yuko
- Mizuguchi, Kenji
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2016-01-20
- Volume
- 25
- Issue
- 4
- Pages
- 815-825
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC4941225
- OpenAlex
- W2246074199
- Cited by
- 86
- References
- 28
- Citations by year
- 2026: 18 · 2025: 12 · 2024: 13 · 2023: 7 · 2022: 6 · 2021: 6 · 2020: 5 · 2019: 9 · 2018: 5 · 2017: 2 · 2016: 3
- FWCI
- 5.49
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Protein Science (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (Grants-in-Aid for Scientific Research) (25430186 and 25293079)
- Japan Agency for Medical Research and Development (“The adjuvant database project”) to K.M
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- hypervariable region, antigen recognition, loop length, antibody-antigen binding
- MeSH terms
- Algorithms, Amino Acid Sequence, Antibodies, Antigens, Models, Molecular, Protein Conformation, Crystallography, X-Ray, Complementarity Determining Regions
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