ArticlePLoS computational biology2020
Comprehensive analysis of structural and sequencing data reveals almost unconstrained chain pairing in TCRαβ complex.
Article in PLoS computational biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Structural T-Cell Receptor Analysis in the Age of Machine Learning.Immunological reviews · 2026Review
- Systematic analysis of CDR contacts and pairing constraints between T cell receptor αβ chains.Bioinformatics (Oxford, England) · 2026Article
- T-cell receptor alpha to beta chains binding prediction.Briefings in bioinformatics · 2026Article
- Computational design of orthogonal TCR α/β interfaces for dual-TCR therapeutics.bioRxiv : the preprint server for biology · 2026Article
- Simulation of adaptive immune receptors and repertoires with complex immune information to guide the development and benchmarking of AIRR machine learning.Nucleic acids research · 2025Article
- Limits on inferring T cell specificity from partial information.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Measures of epitope binding degeneracy from T cell receptor repertoires.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Clustering and Annotation of T Cell Receptor Repertoires.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Inference of B cell clonal families using heavy/light chain pairing information.PLoS computational biology · 2022Article
- Engineering soluble T-cell receptors for therapy.The FEBS journal · 2021Review
- Deep generative selection models of T and B cell receptor repertoires with soNNia.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Biased MAIT TCR Usage Poised for Limited Antigen Diversity?Frontiers in immunology · 2020Review
- Review
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Authors and funding
3 authors.
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Abstract
Antigen recognition by T-cells is guided by the T-cell receptor (TCR) heterodimer formed by α and β chains. A huge diversity of TCR sequences should be maintained by the immune system in order to be able to mount an effective response towards foreign pathogens, so, due to cooperative binding of α and β chains to the pathogen, any constraints on chain pairing can have a profound effect on immune repertoire structure, diversity and antigen specificity. By integrating available structural data and paired chain sequencing results we were able to show that there are almost no constraints on pairing in TCRαβ complexes, allowing naive T-cell repertoire to reach the highest possible diversity. Additional analysis reveals that the specific choice of contacting amino acids can still have a profound effect on complex conformation. Moreover, antigen-driven selection can distort the uniform landscape of chain pairing, while small, yet significant, differences in the pairing can be attributed to various specialized T-cell subsets such as MAIT and iNKT T-cells, as well as other TCR sets specific to certain antigens.
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