ArticleScientific reports2020
T-Cell Receptor Variable β Domains Rigidify During Affinity Maturation.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed.
- Article
- Structure and Dynamics Guiding Design of Antibody Therapeutics and Vaccines.Antibodies (Basel, Switzerland) · 2023Review
- Structural Characterization of Nanobodies during Germline Maturation.Biomolecules · 2023Article
- Specific attributes of the VFrontiers in immunology · 2023Article
- Conformational Entropy as a Potential Liability of Computationally Designed Antibodies.Biomolecules · 2022Article
- Nanobody Paratope Ensembles in Solution Characterized by MD Simulations and NMR.International journal of molecular sciences · 2022Article
- 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
- Computational Construction of a Single-Chain Bi-Paratopic Antibody Allosterically Inhibiting TCR-Staphylococcal Enterotoxin B Binding.Frontiers in immunology · 2021Article
- Antibodies exhibit multiple paratope states influencing VCommunications biology · 2020Article
- Local and Global Rigidification Upon Antibody Affinity Maturation.Frontiers in molecular biosciences · 2020Article
- T-Cell Receptor CDR3 Loop Conformations in Solution Shift the Relative Vα-Vβ Domain Distributions.Frontiers in immunology · 2020Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We investigated T-cell receptor variable β chains binding to the superantigen staphylococcal enterotoxin C3 (SEC 3) with structure information in different stages of affinity maturation. Metadynamics in combination with molecular dynamics simulations allow to access the micro-to-millisecond timescale and reveal a strong effect of energetically significant mutations on the flexibility of the antigen-binding site. The observed changes in dynamics of the complementarity determining region (CDR) loops, especially the CDR 2, and HV 4 loop on this specific pathway of affinity maturation are reflected in their structural diversity, thermodynamics of conformations and kinetics of structural transitions. In addition, this affinity maturation pathway follows the concept of conformational selection, because even without the presence of the antigen the binding competent state is present in this pre-existing ensemble of conformations. In all stages of this affinity maturation process we observe a link between specificity and reduced flexibility.
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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.