ArticleFrontiers in immunology2019
Transitions of CDR-L3 Loop Canonical Cluster Conformations on the Micro-to-Millisecond Timescale.
Article in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Tokenizing loops of antibodies.mAbs · 2026Article
- Structural T-Cell Receptor Analysis in the Age of Machine Learning.Immunological reviews · 2026Review
- AbMelt: Learning antibody thermostability from molecular dynamics.Biophysical journal · 2024Article
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- Structural mechanism of Fab domain dissociation as a measure of interface stability.Journal of computer-aided molecular design · 2023Article
- Conformational Ensembles of Antibodies Determine Their Hydrophobicity.Biophysical journal · 2021Article
- Mutation of Framework Residue H71 Results in Different Antibody Paratope States in Solution.Frontiers in immunology · 2021Article
- Germline-Dependent Antibody Paratope States and Pairing Specific VFrontiers in immunology · 2021Article
- Antibodies exhibit multiple paratope states influencing VCommunications biology · 2020Article
- pH-Induced Local Unfolding of the Phl p 6 Pollen Allergen From cpH-MD.Frontiers in molecular biosciences · 2020Article
- T-Cell Receptor CDR3 Loop Conformations in Solution Shift the Relative Vα-Vβ Domain Distributions.Frontiers in immunology · 2020Article
- Structural Aspects of the Allergen-Antibody Interaction.Frontiers in immunology · 2020Review
- Surprisingly Fast Interface and Elbow Angle Dynamics of Antigen-Binding Fragments.Frontiers in molecular biosciences · 2020Article
- Conformational selection of allergen-antibody complexes-surface plasticity of paratopes and epitopes.Protein engineering, design & selection : PEDS · 2019Article
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Authors and funding
4 authors.
Funding
Abstract
Sequence and structural diversity of antibodies are concentrated on six hypervariable loops, also known as the complementarity determining regions (CDRs). Five of six antibody CDR loops presumably adopt a so-called canonical structure out of a limited number of conformations. However, here we show for four antibody CDR-L3 loops differing in length and sequence, that each loop undergoes conformational transitions between different canonical structures. By extensive sampling in combination with Markov-state models we reconstruct the kinetics and probabilities of the transitions between canonical structures. Additionally, for these four CDR-L3 loops, we identify all relevant conformations in solution. Thereby we extend the model of static canonical structures to a dynamic conformational ensemble as a new paradigm in the field of antibody structure design.
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