ArticleFrontiers in immunology2020
T-Cell Receptor CDR3 Loop Conformations in Solution Shift the Relative Vα-Vβ Domain Distributions.
Article in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 27 citations in OpenAlex.
- Structural T-Cell Receptor Analysis in the Age of Machine Learning.Immunological reviews · 2026Review
- T-cell receptor insights: Determinants of Major Histocompatibility Complex class I versus class II recognition.Protein science : a publication of the Protein Society · 2025Article
- Analysis of Vβ-Segment Diversity of T-cell Receptor in Techa Riverside Residents Chronically Exposed to Radiation in the Long-Term Period.Doklady. Biochemistry and biophysics · 2025Article
- Analysis of Vβ-Segment Diversity of T-Cell Receptor in Residents of the Techa Riverside Villages Chronically Exposed to Radiation in the Long-Term Period.Doklady. Biochemistry and biophysics · 2025Article
- Can AlphaFold's breakthrough in protein structure help decode the fundamental principles of adaptive cellular immunity?Nature methods · 2024Review
- Quantifying conformational changes in the TCR:pMHC-I binding interface.Frontiers in immunology · 2024Article
- Enhanced T cell receptor specificity through framework engineering.Frontiers in immunology · 2024Article
- Article
- Defining and Studying B Cell Receptor and TCR Interactions.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Large-Scale Ligand Perturbations of the Protein Conformational Landscape Reveal State-Specific Interaction Hotspots.Journal of medicinal chemistry · 2022Article
- Structural insights into engineering a T-cell receptor targeting MAGE-A10 with higher affinity and specificity for cancer immunotherapy.Journal for immunotherapy of cancer · 2022Article
- Nanobody Paratope Ensembles in Solution Characterized by MD Simulations and NMR.International journal of molecular sciences · 2022Article
- Article
- The influence of antibody humanization on shark variable domain (VNAR) binding site ensembles.Frontiers in immunology · 2022Article
- Mutation of Framework Residue H71 Results in Different Antibody Paratope States in Solution.Frontiers in immunology · 2021Article
- Shark Antibody Variable Domains Rigidify Upon Affinity Maturation-Understanding the Potential of Shark Immunoglobulins as Therapeutics.Frontiers in molecular biosciences · 2021Article
- Germline-Dependent Antibody Paratope States and Pairing Specific VFrontiers in immunology · 2021Article
- Antibodies exhibit multiple paratope states influencing VCommunications biology · 2020Article
- Surprisingly Fast Interface and Elbow Angle Dynamics of Antigen-Binding Fragments.Frontiers in molecular biosciences · 2020Article
- Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
T-cell receptors are an important part in the adaptive immune system as they are responsible for detecting foreign proteins presented by the major histocompatibility complex (MHC). The affinity is predominantly determined by structure and sequence of the complementarity determining regions (CDRs), of which the CDR3 loops are responsible for peptide recognition. We present a kinetic classification of T-cell receptor CDR3 loops with different loop lengths into canonical and non-canonical solution structures. Using molecular dynamics simulations, we do not only sample available X-ray structures, but we also observe a substantially broader CDR3 loop ensemble with various distinct kinetic minima in solution. Our results strongly imply, that for given CDR3 loop sequences several canonical structures have to be considered to characterize the conformational diversity of these loops. Our suggested dominant solution structures could extend the repertoire of available canonical clusters by including kinetic minimum structures present in solution. Thus, the CDR3 loops need to be characterized as conformational ensembles in solution. Furthermore, the conformational changes of the CDR3 loops follow the paradigm of conformational selection, because the experimentally determined binding competent state is present within this ensemble of pre-existing conformations without the presence of the antigen. We also identify strong correlations between the CDR3 loops and include combined state descriptions. Additionally, we observe a strong dependency of the CDR3 loop conformations on the relative Vα-Vβ interdomain orientations, revealing that certain CDR3 loop states favor specific interface orientations.
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