ArticleThe EMBO journal1995
The structural repertoire of the human V kappa domain.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Selection of a PD-1 blocking antibody from a novel fully human phage display library.Protein science : a publication of the Protein Society · 2022Article
- Evolution of Anti-SARS-CoV-2 Therapeutic Antibodies.International journal of molecular sciences · 2022Review
- Quantitative Description of Surface Complementarity of Antibody-Antigen Interfaces.Frontiers in molecular biosciences · 2021Article
- Human fibronectin extra domain B as a biomarker for targeted therapy in cancer.Molecular oncology · 2020Review
- Antibody Structure and Function: The Basis for Engineering Therapeutics.Antibodies (Basel, Switzerland) · 2019Review
- Structures of the antibody 64M-5 Fab and its complex with dT(6-4)T indicate induced-fit and high-affinity mechanisms.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Transitions of CDR-L3 Loop Canonical Cluster Conformations on the Micro-to-Millisecond Timescale.Frontiers in immunology · 2019Article
- Predicting B cell receptor substitution profiles using public repertoire data.PLoS computational biology · 2018Article
- Generation and characterisation of recombinant FMDV antibodies: Applications for advancing diagnostic and laboratory assays.PloS one · 2018Article
- PIGSPro: prediction of immunoGlobulin structures v2.Nucleic acids research · 2017Article
- Structural reconstruction of protein ancestry.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Defining the complementarities between antibodies and haptens to refine our understanding and aid the prediction of a successful binding interaction.BMC biotechnology · 2015Article
- Predominant structural configuration of natural antibody repertoires enables potent antibody responses against protein antigens.Scientific reports · 2015Article
- Article
- Antibody modeling using the prediction of immunoglobulin structure (PIGS) web server [corrected].Nature protocols · 2014Article
- Article
- A highly functional synthetic phage display library containing over 40 billion human antibody clones.PloS one · 2014Article
- A complete, multi-level conformational clustering of antibody complementarity-determining regions.PeerJ · 2014Article
- Natural and man-made V-gene repertoires for antibody discovery.Frontiers in immunology · 2012Article
- Phage display-based strategies for cloning and optimization of monoclonal antibodies directed against human pathogens.International journal of molecular sciences · 2012Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In humans, the gene for the V kappa domain is produced by the recombination of one of 40 functional V kappa segments and one of five functional J kappa segments. We have analysed the sequences of these germline segments and of 736 rearranged V kappa genes to determine the repertoire of main chain conformations, or canonical structures, they encode. Over 96% of the sequences correspond to one of four canonical structures for the first antigen binding loop (L1) and one canonical structure for the second antigen binding loop (L2). Junctional diversity produces some variation in the length of the third antigen binding loop (L3) and in the identity of residues at the V kappa-J kappa join. However, this is limited and 70% of the rearranged sequences correspond to one of three known canonical structures for the L3 region. Furthermore, we show that the canonical structures selected during the primary response are conserved during affinity maturation: the key residues that determine the conformations of the antigen binding loops are unmutated or undergo conservative mutation. The implications of these results for immune recognition are discussed.
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