ArticleProtein engineering, design & selection : PEDS2019
Adaption of human antibody λ and κ light chain architectures to CDR repertoires.
Article in Protein engineering, design & selection : PEDS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Deep generative modeling captures maturation-dependent pairing patterns in human antibodies.iScience · 2026Article
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- Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization.Antibodies (Basel, Switzerland) · 2025Article
- Mice carrying the full-length human immunoglobulin loci produce antigen-specific human antibodies with the lambda light chain.iScience · 2024Article
- Contextualising the developability risk of antibodies with lambda light chains using enhanced therapeutic antibody profiling.Communications biology · 2024Article
- Bat humoral immunity and its role in viral pathogenesis, transmission, and zoonosis.Frontiers in immunology · 2024Review
- How can we discover developable antibody-based biotherapeutics?Frontiers in molecular biosciences · 2023Review
- Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains.The Journal of biological chemistryArticle
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies bind with high specificity to a wide range of diverse antigens, primarily mediated by their hypervariable complementarity determining regions (CDRs). The defined antigen binding loops are supported by the structurally conserved β-sandwich framework of the light chain (LC) and heavy chain (HC) variable regions. The LC genes are encoded by two separate loci, subdividing the entity of antibodies into kappa (LCκ) and lambda (LCλ) isotypes that exhibit distinct sequence and conformational preferences. In this work, a diverse set of techniques were employed including machine learning, force field analysis, statistical coupling analysis and mutual information analysis of a non-redundant antibody structure collection. Thereby, it was revealed how subtle changes between the structures of LCκ and LCλ isotypes increase the diversity of antibodies, extending the predetermined restrictions of the general antibody fold and expanding the diversity of antigen binding. Interestingly, it was found that the characteristic framework scaffolds of κ and λ are stabilized by diverse amino acid clusters that determine the interplay between the respective fold and the embedded CDR loops. In conclusion, this work reveals how antibodies use the remarkable plasticity of the beta-sandwich Ig fold to incorporate a large diversity of CDR loops.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.