ArticlePLoS computational biology2014
Examining variable domain orientations in antigen receptors gives insight into TCR-like antibody design.
Article in PLoS computational biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- T cell receptor therapeutics: immunological targeting of the intracellular cancer proteome.Nature reviews. Drug discovery · 2023Review
- Computationally profiling peptide:MHC recognition by T-cell receptors and T-cell receptor-mimetic antibodies.Frontiers in immunology · 2022Article
- Peptide Centric Vβ Specific Germline Contacts Shape a Specialist T Cell Response.Frontiers in immunology · 2022Article
- Broad specificity of immune helminth scFv library to identify monoclonal antibodies targeting Strongyloides.Scientific reports · 2021Article
- Molecular Insights of Nickel Binding to Therapeutic Antibodies as a Possible New Antibody Superantigen.Frontiers in immunology · 2021Article
- Specificity of bispecific T cell receptors and antibodies targeting peptide-HLA.The Journal of clinical investigation · 2020Article
- T-Cell Receptor CDR3 Loop Conformations in Solution Shift the Relative Vα-Vβ Domain Distributions.Frontiers in immunology · 2020Article
- Comparative Analysis of the CDR Loops of Antigen Receptors.Frontiers in immunology · 2019Article
- Opportunities and Challenges for Antibodies against Intracellular Antigens.Theranostics · 2019Review
- STCRDab: the structural T-cell receptor database.Nucleic acids research · 2018Article
- DynaDom: structure-based prediction of T cell receptor inter-domain and T cell receptor-peptide-MHC (class I) association angles.BMC structural biology · 2017Article
- How structural adaptability exists alongside HLA-A2 bias in the human αβ TCR repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Exploring peptide/MHC detachment processes using hierarchical natural move Monte Carlo.Bioinformatics (Oxford, England) · 2016Article
- Quantitative Analysis of the Association Angle between T-cell Receptor Vα/Vβ Domains Reveals Important Features for Epitope Recognition.PLoS computational biology · 2015Article
- 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
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The variable domains of antibodies and T-Cell receptors (TCRs) share similar structures. Both molecules act as sensors for the immune system but recognise their respective antigens in different ways. Antibodies bind to a diverse set of antigenic shapes whilst TCRs only recognise linear peptides presented by a major histocompatibility complex (MHC). The antigen specificity and affinity of both receptors is determined primarily by the sequence and structure of their complementarity determining regions (CDRs). In antibodies the binding site is also known to be affected by the relative orientation of the variable domains, VH and VL. Here, the corresponding property for TCRs, the Vβ-Vα orientation, is investigated and compared with that of antibodies. We find that TCR and antibody orientations are distinct. General antibody orientations are found to be incompatible with binding to the MHC in a canonical TCR-like mode. Finally, factors that cause the orientation of TCRs and antibodies to be different are investigated. Packing of the long Vα CDR3 in the domain-domain interface is found to be influential. In antibodies, a similar packing affect can be achieved using a bulky residue at IMGT position 50 on the VH domain. Along with IMGT VH 50, other positions are identified that may help to promote a TCR-like orientation in antibodies. These positions should provide useful considerations in the engineering of therapeutic TCR-like antibodies.
Indexed as
Identifiers
What OpenQuestion holds
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.